Pullulanase variants and methods for preparing such variants with predetermined properties

ABSTRACT

The inventors have modified the amino acid sequence of a pullulanase to obtain variants with improved properties, based on the three-dimensional structure of the pullulanase Promozyme®. The variants have altered physicochemical properties, e.g. an altered pH optimum, improved thermostability, altered substrate specificity, increased specific activity or an altered cleavage pattern.

CROSS-REFERENCE TO RELATED APPLICATIONS

This application claims priority under 35 U.S.C. 119 of Danish application PA 2000 00045 filed Jan. 12, 2000, the contents of which are fully incorporated herein by reference.

FIELD OF THE INVENTION

The present invention relates to variants of pullulanases and to methods for constructing such variants.

BACKGROUND OF THE INVENTION

Starches such as corn, potato, wheat, manioc and rice starch are used as the starting material in commercial large scale production of sugars, such as high fructose syrup, high maltose syrup, maltodextrins, amylose, G4-G6 oligosaccharides and other carbohydrate products such as fat replacers.

Degradation of Starch

Starch usually consists of about 80% amylopectin and 20% amylose. Amylopectin is a branched polysaccharide in which linear chains α-1,4 D-glucose residues are joined by α-1,6 glucosidic linkages. Amylopectin is partially degraded by α-amylase, which hydrolyzes the 1,4-α-glucosidic linkages to produce branched and linear oligosaccharides. Prolonged degradation of amylopectin by α-amylase results in the formation of so-called α-limit dextrins which are not susceptible to further hydrolysis by the α-amylase. Branched oligosaccharides can be hydrolyzed into linear oligosaccharides by a debranching enzyme. The remaining branched oligosaccharides can be depolymerized to D-glucose by glucoamylase, which hydrolyzes linear oligosaccharides into D-glucose.

Amylose is a linear polysaccharide built up of D-glucopyranose units linked together by α-1,4 glucosidic linkages. Amylose is degraded into shorter linear oligosaccharides by α-amylase, the linear oligosaccharides being depolymerized into D-glucose by glucoamylase.

In the case of converting starch into a sugar, the starch is depolymerized. The depolymerization process consists of a pretreatment step and two or three consecutive process steps, namely a liquefaction process, a saccharification process and, depending on the desired end product, optionally an isomerization process.

Pre-treatment of Native Starch

Native starch consists of microscopic granules which are insoluble in water at room temperature. When an aqueous starch slurry is heated, the granules swell and eventually burst, dispersing the starch molecules into the solution. During this “gelatinization” process there is a dramatic increase in viscosity. As the solids level is 30-40% in a typical industrial process, the starch has to be thinned or “liquefied” so that it can be handled. This reduction in viscosity is today mostly obtained by enzymatic degradation.

Liquefaction

During the liquefaction step, the long-chained starch is degraded into smaller branched and linear units (maltodextrins) by an α-amylase (e.g. Termamyl™, available from Novo Nordisk A/S, Denmark). The liquefaction process is typically carried out at about 105-110° C. for about 5 to 10 minutes followed by about 1-2 hours at about 95° C. The pH generally lies between about 5.5 and 6.2. In order to ensure an optimal enzyme stability under these conditions, calcium is added, e.g. 1 mM of calcium (40 ppm free calcium ions). After this treatment the liquefied starch will have a “dextrose equivalent” (DE) of 10-15.

Saccharification

After the liquefaction process the maltodextrins are converted into dextrose by addition of a glucoamylase (e.g. AMG™, available from Novo Nordisk A/S) and a debranching enzyme, such as an isoamylase (see e.g. U.S. Pat. No. 4,335,208) or a pullulanase (e.g. Promozyme®, available from Novo Nordisk A/S; see U.S. Pat. No. 4,560,651). Before this step the pH is reduced to a value below 4.5, e.g. about 3.8, maintaining the high temperature (above 95° C.) for a period of e.g. about 30 min. to inactivate the liquefying α-amylase to reduce the formation of short oligosaccharides called “panose precursors” which cannot be hydrolyzed properly by the debranching enzyme.

The temperature is then lowered to 60° C., glucoamylase and debranching enzyme are added, and the saccharification process proceeds for about 24-72 hours.

Normally, when denaturing the α-amylase after the liquefaction step, a small amount of the product comprises panose precursurs which cannot be degraded by pullulanases or AMG. If active amylase from the liquefaction step is present during saccharification (i.e. no denaturing), this level can be as high as 1-2% or even higher, which is highly undesirable as it lowers the saccharification yield significantly. For this reason, it is also preferred that the α-amylase is one which is capable of degrading the starch molecules into long, branched oligosaccharides (such as, e.g., the Fungamyl™-like α-amylases) rather than shorter branched oligosaccharides.

Isomerization

When the desired final sugar product is e.g. high fructose syrup, the dextrose syrup may be converted into fructose by enzymatic isomerization. After the saccharification process the pH is increased to a value in the range of 6-8, preferably about pH 7.5, and the calcium is removed by ion exchange. The dextrose syrup is then converted into high fructose syrup using, e.g., an immobilized glucose isomerase (such as Sweetzyme™, available from Novo Nordisk A/S).

Debranching Enzymes

Debranching enzymes which can attack amylopectin are divided into two classes: isoamylases (E.C. 3.2.1.68) and pullulanases (E.C. 3.2.1.41), respectively. Isoamylase hydrolyses α-1,6-D-glucosidic branch linkages in amylopectin and β-limit dextrins and can be distinguished from pullulanases by the inability of isoamylase to attack pullulan, and by their limited action on α-limit dextrins.

When an acidic stabilized α-amylase is used for the purpose of maintaining the amylase activity during the entire saccharification process (no inactivation), the degradation specificity should be taken into consideration. It is desirable in this regard to maintain the α-amylase activity throughout the saccharification process, since this allows a reduction in the amyloglucidase addition, which is economically beneficial and reduces the AMG™ condensation product isomaltose, thereby increasing the DE (dextrose equivalent) yield.

It will be apparent from the above discussion that the known starch conversion processes are performed in a series of steps, due to the different requirements of the various enzymes in terms of e.g. temperature and pH. It would therefore be desirable to be able to engineer one or more of these enzymes, e.g. pullulanases, so that the overall process could be performed in a more economical and efficient manner. One possibility in this regard is to engineer the otherwise thermolabile pullulanases so as to render them more stable at higher temperatures.

BRIEF DISCLOSURE OF THE INVENTION

The inventors have modified the amino acid sequence of a pullulanase to obtain variants with improved properties, based on the three-dimensional structure of the pullulanase Promozyme® (available from Novo Nordisk A/S). The variants have altered physicochemical properties, e.g. an altered pH optimum, improved thermostability, increased specific activity or an altered cleavage pattern.

Accordingly, the object of the present invention is to provide a method for constructing pullulanases having altered properties, in particular to provide a method for constructing pullulanases having improved thermostability, altered pH dependent activity and/or altered substrate specificity, such as increased isoamylase activity.

Thus, in its broadest aspect, the present invention relates to a method for constructing a variant of a parent pullulanase, wherein the variant has at least one altered property as compared to said parent pullulanase, which method comprises:

i) analyzing the structure of the pullulanase to identify, on the basis of an evaluation of structural considerations, at least one amino acid residue or at least one structural region of the pullulanase, which is of relevance for altering said property;

ii) constructing a variant of the pullulanase, which as compared to the parent pullulanase, has been modified in the amino acid residue or structural part identified in i) so as to alter said property; and

iii) testing the resulting pullulanase variant for said property.

The property which may be altered by the above methods of the present invention may be, e.g., thermostability, pH dependent activity, specific activity, or substrate specificity. Thus, the variant may have, e.g., increased thermostability, higher activity at a lower pH, an altered pH optimum, improved thermostability, or increased specific activity, such as increased isoamylase activity.

Although it has been described in the following that modification of the parent pullulanase in certain regions and/or positions is expected to confer a particular effect to the thus produced pullulanase variant (such as an improved thermostability or an increased isoamylase activity), it should be noted that modification of the parent pullulanase in any of such regions may also give rise to any other of the above-mentioned effects. For example, any of the regions and/or positions mentioned as being of particular interest with respect to, e.g., improved thermostability, may also give rise to, e.g., higher activity at a lower pH, an altered pH optimum, or increased specific activity, such as increased isoamylase activity.

Further aspects of the present invention relates to variants of a pullulanase, the DNA encoding such variants and methods of preparing the variants. Still further aspects of the present invention relates to the use of the variants for various industrial purposes, in particular for processes where sweeteners are made from starch. Other aspects of the present invention will be apparent from the below description as well as from the appended claims.

BRIEF DESCRIPTION OF THE DRAWINGS

FIG. 1 shows the DNA plasmid pCA36 harboring the gene encoding the pullulanase from Bacillus deramificans (SEQ ID NO: 3).

DETAILED DISCLOSURE OF THE INVENTION

Pullulanases

As explained above, pullulanases are enzymes classified in EC 3.2.1.41 and such enzymes are characterized by their ability to hydrolyze the α-1,6-glycosidic bonds in, for example, amylopectin and pullulan.

A particularly interesting pullulanase is the pullulanase from Bacillus acidopullulyticus described in U.S. Pat. No. 4,560,651 (hereinafter referred to as Promozyme®). Promozyme® has the amino acid sequence set forth in amino acids 1-921 of SEQ ID NO: 1. The three-dimensional structure of Promozyme® is described below.

Another interesting pullulanase is the pullulanase from Bacillus deramificans described in U.S. Pat. No. 5,736,375. This enzyme has the amino acid sequence set forth in amino acid sequence 1-928 of SEQ ID NO: 3. Homology building of the tree-dimensional structure of the above-mentioned pullulanase is described below.

In general, a preferred pullulanase suitable for the purpose described herein should have one or more of the following properties:

i) A three-dimensional structure homologous to Promozyme®.

ii) An amino acid sequence which is at least 40% homologous to SEQ ID NO:1 or SEQ ID NO:3, preferably at least 50%, e.g. at least 60%, such as a least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% homologous to SEQ ID NO:1 or SEQ ID NO:3.

iii) A nucleic acid sequence which hybridizes to the nucleic acid sequence set forth in SEQ ID NO:1 or SEQ ID NO:3.

The structural homology referred to above in i) above is based on other sequence homologies, hydrophobic cluster analysis or by reverse threading (Huber, T; Torda, A E, PROTEIN SCIENCE Vol. 7, No. 1 pp. 142-149 (1998)) and which by any of these methods is predicted to have the same tertiary structure as Promozyme, wherein the tertiary structure refers to the overall folding or the folding of Domains N1, N2, A, B, and C. Alternatively, a structural alignment between Promozyme and homologous sequences may be used to identify equivalent positions.

For example, the homology between various pullulanase with known amino acid sequence has been compiled in the below matrix:

1 2 3 4 5 6 7 8 9 10 1. pula_kleae 100 86 59 51 52 5.3 52 52 55 50 2. pula_klepn 100 58 51 51 53 53 53 53 52 3. w81973 100 55 56 52 55 54 51 56 4. r56989 100 98 60 76 54 56 76 5. sp929mat 100 61 78 54 57 78 6. fervido_x 100 61 57 54 62 7. sp734 100 56 54 91 8. r71616 100 54 56 9. w09257 100 54 10. Promozyme ® 100 1. Pula_kleae: Pullulanase from Klebsiella aerogenes (J. Bacteriol. (1987) 169;2301-2306). 2. Pula_klepn: Pullulanase from Klebsiella pneumonia (Mol Microbiol. (1990)4, 73-85; J Bacteriol. (1985) 164, 639-645; J. Bacteriol. (1989) 171, 3673-3679). 3. W81973: Pullulanase fragment from zea mays (WO 98/50562). 4. r56989: Mature pullulanase from Bacillus deramificans T 89.117D (EP 0 605 040). 5. sp929mat: Mature part of pullulanase from Bacillus deramificans (US 5,736,375). 6. fervido_x: Mature part of pullulanase from Fervidobacterium pennavorans Ven5 (Appl. Environ. Microb. (1997) 63, 1088-1094). 7. sp734: Mature pullulanase from Bacillus acidopullulyticus (FEMS Mic. Let. (1994) 115, 97-106. 8. r71616: Pullulanase from Thermus sp. (JP 07023783). 9. w09257: Pullulanase from Bacillus sp. KSM-AP 1378 (WO 96135794).

The above homology calculations were determined by use of the GAP program from the UWGCG package using default values for GAP penalties, i.e. GAP creation penalty of 3.0 and GAP extension penalty of 0.1 (Program Manual for the Wisconsin Package, Version 8, August 1994, Genetics Computer Group, 575 Science Drive, Madison, Wis., USA 53711).

A sequence alignment between Promozyme® (SEQ ID NO: 1), the pullulanase from Bacillus deramificans (SEQ ID NO: 3) and the pullulanase from Bacillus acidopullulyticus (SEQ ID NO: 5) described in FEMS Mic. Let. (1994) 115, 97-106, is shown in Appendix 2.

Three-dimensional Structure of Pullulanase

Promozyme® was used to elucidate the three-dimensional structure forming the basis for the present invention.

The structure of Promozyme® was solved in accordance with the principle for x-ray crystallographic methods, for example, as given in X-Ray Structure Determination, Stout, G. K. and Jensen, L. H., John Wiley & Sons, Inc. NY, 1989.

The structural coordinates for the solved crystal structure of Promozyme® using the isomorphous replacement method are given in standard PDB format (Protein Data Bank, Brookhaven National Laboratory, Brookhaven, Conn.) as set forth in Appendix 1. It is to be understood that Appendix 1 forms part of the present application. In the context of Appendix 1, the following abbreviations are used: WAT refers to water or to calcium. Amino acid residues are given in their standard three letter code.

The structure of said Pullulanase is made up of five globular domains, ordered N1, N2, A, B, and C. The domains can be defined as being residues 1-310 for domain N1, 311-420 for Domain N2, residues 421-556 and 596-835 for domain A, residues 557-595 for Domain B, residues 596-922 for Domain C, wherein the numbering refers to the amino acid sequence in SEQ ID NO: 1. Features of Domains N1, A, B and C of particular interest are described below.

Domain N1

Domain N1 contains in this particular pullulanase an extra loop of 100 residues compared to the pullulanase from Bacillus acidopullulyticus having the amino acid sequence shown in SEQ ID NO: 5. The loop is also present in the pullulanase from Bacillus deramificans having the amino acid sequence shown in SEQ ID NO: 3.

Part of the N2 domain is homologeous to the N1 domain of Pseudomonase amyloderamosa isoamylase (1bf2.pdb from Brookhaven database).

Domain A

Domain A is the largest domain and contains the active site which comprises a cluster of three amino acid residues, D622, D736 and E651, spatially arranged at the bottom of a cleft in the surface of the enzyme. The structure of Domain A shows an overall fold in common with the α-amylases for which the structure is known, viz. the (beta/alpha) 8 barrel with eight central beta strands (numbered 1-8) and eight flanking a-helices. The β-barrel is defined by McGregor, J. Prot. Chem. 7:399, 1988. The C-terminal end of the beta strand 1 is connected to helix 1 by a loop denoted loop 1 and an identical pattern is found for the other loops, although the loops show some variation in size and some can be quite extensive.

The eight central beta-strands in the (beta/alpha) 8 barrel superimpose reasonably well with the known structures of family 13 (Henrissat B. Biochem. J. (1991) 280, 309-316 and Henrissat B. and Bairoch A. Biochem. J. (1993) 293, 781-788). This part of the structure, including the close surroundings of the active site located at the C-terminal end of the beta-strands, shows a high degree of homology with isoamylases.

In contrast, the loops connecting the beta-strands and alpha helices display a high degree of variation from the known structures of family 13 enzymes. These loops constitute the structural context of the active site, and the majority of the contacts to the substrate is found among residues located in these loops. Distinguishing characteristics such as substrate specificity, substrate binding, pH activity profile, substrate cleavage pattern, and the like, are determined by specific amino acids and the positions they occupy in these loops.

Domain B

Domain B, also referred to as loop 3 of the (beta/alpha) 8 barrel, in comprises amino acid residues 557-595 of the amino acid sequence shown in SEQ ID NO: 1. The most striking difference to other family 13 enzymes being the short amino acid sequence. This short sequence loop are of the same size as the isoamylase loop 3 and spatially positioned close to the active site residues and in close contact to the substrate.

Domain C

Domain C in Promozyme comprises amino acid residues 596-922 of the amino acid sequence shown in SEQ ID NO: 1. Domain C is composed entirely of β-strands which form a single 8-stranded sheet structure that folds back on itself, and thus may be described as a β-sandwich structure. One part of the β-sheet forms the interface to Domain A.

Substrate Binding Site

Parts of the loop discussed above in the context of domains A, B and N2 are of particular interest for substrate interaction and active site reactivity. In particular, in domain A, residues 439-443 in loop 1, residues 490-514 in loop 2, residues 621-628 in loop 4, residues 652-668 in loop 5, residues 679-694 in loop 6, residues 733-740 in loop 7 and residues 787-796 in loop 8; in domain B, residues 553-564 and 581-592 in loop 3; in domain N2, residues 400-404, wherein residue positions correspond to the amino acids in the amino acid sequence in SEQ ID NO: 1.

Homology Building of Bacillus deramificans Pullulanase or Other Pullulanases

The structure of the Bacillus deramificans pullulanase (SEQ ID NO:3) was model built on the structure disclosed in Appendix 1 herein. The structure of other pullulanases may be built analogously.

A model structure of a pullulanase can be built using the Homology program or a comparable program, e.g., Modeller (both from Molecular Simulations, Inc., San Diego, Calif.). The principle is to align the sequence of the pullulanase with the known structure with that of the pullulanase for which a model structure is to be constructed. The structurally conserved regions can then be built on the basis of consensus sequences. In areas lacking homology, loop structures can be inserted, or sequences can be deleted with subsequent bonding of the necessary residues using, e.g., the program Homology. Subsequent relaxing and optimization of the structure should be done using either Homology or another molecular simulation program, e.g., CHARMm from Molecular Simulations.

Methods for Designing Novel Pullulanase Variants

In a first aspect, the present invention relates to a method for producing a variant of a parent pullulanase, wherein the variant has at least one altered property as compared to the parent pullulanase, the method comprising:

i) modeling the parent pullulanase on the three-dimensional structure of SEQ ID NO: 1 depicted in Appendix 1 to produce a three-dimensional structure of the parent pullulanase;

ii) identifying in the three-dimensional structure obtained in step (i) at least one structural part of the parent pullulanase, wherein an alteration in the structural part is predicted to result in an altered property;

iii) modifying the nucleic acid sequence encoding the parent pullulanase to produce a nucleic acid sequence encoding a deletion, insertion, or substitution of one or more amino acids at a position corresponding to the structural part; and

iv) expressing the modified nucleic acid sequence in a host cell to produce the variant pullulanase.

The structural part which is identified in step ii) of the method of the invention may be composed of one amino acid residue. Normally, however, the structural part comprises more than one amino acid residue, typically constituting one of the above-mentioned parts of the pullulanase structure such as one of the N1, N2, A, B, or C domains, an interface between any of these domains, a calcium binding site, a loop structure, the substrate binding site, or the like.

The structural or functional considerations may involve an analysis of the relevant structure or structural part and its contemplated impact on the function of the enzyme. For example, an analysis of the functional differences between pullulanases and the various isoamylases may be used for assigning certain properties of Promozyme® or homologeous model builded structure to certain parts of the Promozyme® or homologeous model builded structure or to contemplate such relationship. For instance, differences in the pattern or structure of loops surrounding the active site may result in differences in access to the active site of the substrate and thus differences in substrate specificity and/or cleavage pattern.

Furthermore, parts of a pullulanase involved in substrate binding, and thus, for example, substrate specificity and/or cleavage, thermostability, and the like, have been identified (vide infra).

The modification of an amino acid residue or structural region is typically accomplished by suitable modifications of a nucleic acid sequence encoding the parent enzyme in question. The modification may be substitution, deletion or insertion of an amino acid residue or a structural part.

The property to be modified may be stability (e.g. thermostability), pH dependent activity, substrate specificity, such as decreased condensation reactions, isoamylase like activity etc. Thus, the altered property may be an altered specific activity at a given pH and/or altered substrate specificity, such as an altered pattern of substrate cleavage or an altered pattern of substrate inhibition.

In step ii) of the method according to the invention the part of the structure to be identified is preferably one which in the folded enzyme is believed to be in contact with the substrate (cf. the disclosure above in the section entitled “Substrate Binding Site”) or involved in substrate specificity and/or cleavage pattern, and/or one which is contributing to the pH or temperature profile of the enzyme, or is otherwise responsible for the properties of the pullulanase.

Described in the following are specific types of variants which have been designed by use of the method of the invention.

The variants of the invention may comprise additional modifications in addition to the modifications described herein. The variants preferably have an amino acid sequence having more than 40% homology with SEQ ID NO: 1, SEQ ID NO: 3, or SEQ ID NO: 5, preferably more than 50%, e.g. more than 60%, such as more than 70%, more than 75%, more than 80%, more than 85%, more than 90%, more than 91%, more than 92%, more than 93%, more than 94%, more than 95%, more than 96%, more than 97%, more than 98% or more than 99% homology with the amino acid sequences shown in SEQ ID NO: 1, SEQ ID NO: 3 or SEQ ID NO: 5.

In the present context the term “homologous to” or “homology” (also sometimes referred to as “similarity”) is used in it conventional meaning and the “homology” between two amino acid sequences may be determined by use of any conventional algorithm, preferably by use of the GAP program from the UWGCG package using default values for GAP penalties, i.e. GAP creation penalty of 3.0 and GAP extension penalty of 0.1 (Program Manual for the Wisconsin Package, Version 8, August 1994, Genetics Computer Group, 575 Science Drive, Madison, Wis., USA 53711). The method is also described in S. B. Needleman and C. D. Wunsch, Journal of Molecular Biology, 48, 443-445 (1970).

As mentioned above, the property to be modified may be stability (e.g. thermostability), pH dependent activity, substrate specificity, such as increased isoamylase activity, or specific activity. Thus, the altered property may be an altered specific activity at a given pH and/or an altered substrate specificity, such as an altered pattern of substrate cleavage or an altered pattern of substrate inhibition.

In a particular interesting embodiment of the invention the property to be modified is the thermostability of the enzyme.

In the present context, the term “thermostable” (or “thermostability”) refers in general to the fact that the pullulanase variants according to the invention have an improved thermostability compared to the relevant parent pullulanase. The degree of improvement in thermostability can vary according to factors such as the thermostability of the parent pullulanase and the intended use of the pullulanase variant, i.e. whether it is primarily intended to be used for liquefaction or for saccharification or both. It will be apparent from the discussion below that for saccharification, the enzyme variant should maintain a substantial degree of enzyme activity during the saccharification step at a temperature of at least about 63° C., preferably at least about 70° C., while an enzyme variant designed for use in the liquefaction step should be able to maintain a substantial degree of enzyme activity at a temperature of at least about 95° C.

The improved thermostability of enzyme variants according to the invention can in particular be defined according to one or more of the following criteria:

In one embodiment, the pullulanase variant of the invention has an improved thermostability (and/or the method of the invention provides a pullulanase with an improved thermostability) as defined by differential scanning calorimetry (DSC) using the method described herein.

In another embodiment, the pullulanase variant of the invention has an improved thermostability (and/or the method of the invention provides a pullulanase with an improved thermostabilty) as defined by an increased half-time (T_(½)) of at least about 5%, preferably at least about 10%, more preferably at least about 15%, more preferably at least about 25%, most preferably at least about 50%, such as at least about 100%, in the “T_(½) assay for liquefaction” described herein, using a pH of 5.0 and a temperature of 95° C. Pullulanase variants according to this definition are suitable for use in the liquefaction step of the starch conversion process.

Alternatively or additionally, a pullulanase variant suitable for use in liquefaction can be defined as having an improved thermostability as defined by an increased residual enzyme activity of at least about 5%, preferably at least about 10%, more preferably at least about 15%, more preferably at least about 25%, most preferably at least about 50%, such as at least about 100%, in the “assay for residual activity after liquefaction” described herein, using a pH of 5.0 and a temperature of 95° C.

In a further embodiment, the enzyme variant of the invention has an improved thermostability (and/or the method of the invention provides a pullulanase with an improved thermostabilty) as defined by an increased half-time (T_(½)) of at least about 5%, preferably at least about 10%, more preferably at least about 15%, more preferably at least about 25%, most preferably at least about 50%, such as at least about 100%, in the “T_(½) assay for saccharification” described herein, using a pH of 4.5 and a temperature of 70° C. Such variants are suitable for use in the saccharification step of the starch conversion process.

Alternatively or additionally, a pullulanase variant suitable for saccharification can be defined as having an improved thermostability as defined by an increased residual enzyme activity of at least about 5%, preferably at least about 10%, more preferably at least about 15%, more preferably at least about 25%, most preferably at least about 50%, such as at least about 100%, in the “assay for residual activity after saccharification” described herein, using a pH of 4.5 and a temperature of 63° C. Preferably, this improved thermostability is also observed when assayed at a temperature of 70° C.

The term “substantially active” as used herein for a given pullulanase variant and a given set of conditions of temperature, pH and time means that the relative enzymatic activity of the enzyme variant is at least about 25%, preferably at least about 50%, in particular at least about 60%, especially at least about 70%, such as at least about 90% or 95%, e.g. at least about 99% compared to the relative activity of the parent enzyme tested under the same set of conditions.

One advantage of the thermostable pullulanase of the invention is that they make it possible to perform liquefaction and debranching simultaneously before the saccharification step. This has not previously been possible, since the known pullulanases with acceptable specific activity are thermolabile and are inactivated at temperatures above 60° C. (Some thermostable pullulanases from Pyrococcus are known, but these have an extremely low specific activity at higher temperatures and are thus unsuitable for purposes of the present invention). By debranching, using the thermostable pullulanases of the invention, during liquefaction together with the action of an α-amylase, the formation of panose precursors is reduced, thereby reducing the panose content in the final product and increasing the overall saccharification yield. It is also possible in this manner to extend the liquefaction process time without risking formation of large amount of panose precursors. By prolonging the liquefaction step, the DE yield is increased from 10-15 to e.g. 15-20, reducing the need for glucoamylase. This reduced glucoamylase requirement is in turn advantageous as the formation of undesired isomaltose is reduced, thereby resulting in an increased glucose yield. In addition, the reduced glucoamylase addition enables the saccharification step to be carried out at a higher substrate concentration (higher DS, dry substances, concentration) than the normal approx. 30-35% used according to the prior art. This allows reduced evaporation costs downstream, e.g. in a high fructose corn syrup process, and the saccharification reaction time can also be reduced, thereby increasing production capacity. A further advantage is that α-amylase used in the liquefaction process does not need to be inactivated/denatured in this case.

Furthermore, it is also possible to use the thermostable pullulanases of the invention during saccharification, which is advantageous for several reasons. In the conventional starch saccharification process, the process temperature is not more than 60° C. due to the fact that neither the saccharification enzyme pullulanase nor AMG™ are sufficiently thermostable to allow the use of a higher temperature. This is a disadvantage, however, as it would be very desirable to run the process at a temperature of above about 60° C., in particular above 63° C., e.g. about 70° C., to reduce microbial growth during the relatively long saccharification step. Furthermore, a higher process temperature normally gives a higher activity per mg of enzyme (higher specific activity), thereby making it possible to reduce the weight amount of enzyme used and/or obtain a higher total enzymatic activity. A higher temperature can also result in a higher dry matter content after saccharification, which would be beneficial in terms of reducing evaporation costs.

In another interesting embodiment of the invention the property to be modified is the substrate specificity of the pullulanase, in particular to modify the substrate specificity of the pullulanase in such a way the variant pullulanase becomes more “isoamylase-like” in the sense of having an increased activity towards high molecular weight branched starchy material such as glycogen and amylopectin. Methods for determining the substrate specificity of pullulanases are discussed in the following section entitled “Methods for determing stability, activity and specificity”.

Thus, when used herein, the term “increased isoamylase activity” refers in general to the fact that the pullulanase variants according to the invention exhibits a higher activity towards high molecular weight branched starchy material, such as glycogen and amylopectin as compared to the parent pullulanase.

The increased isoamylase activity of the pullulanase variants according to the invention can in particular be defined according to the below criteria:

In one embodiment the pullulanase variant according to the invention has an increased isoamylase activity as defined by an increase of at least 5%, preferably of at least 10%, more preferably of at least 15%, more preferably of at least 25%, most preferably of at least 50%, in particular of at least 75%, such as of at least 100% in the number of reducing ends formed in the “assay for isoamylase-like activity” described herein, using 50 mM sodium acetate, a pH of 4.5, 5.0 or 5.5, a temperature of 60° C. and when incubated with a 10 w/v rabbit liver glycogen solution for a period of 10 min.

In the present context the term “pullulanase activity” is intended to mean that the pullulanase variant in question is capable of degrading pullulan when tested as described in the Examples (see the section entitled “Determination of pullulanase activity).

Methods for Determining Stability, Activity and Specificity Thermostability

Thermostability of pullulanases can be detected by measuring the residual activity by incubating the enzyme under accelerated stress conditions, which comprise: pH 4.5 in a 50 mM sodium acetate buffer without a stabilizing dextrin matrix (such as the approximately 35% dry matter which is normally present during saccharification). The stability can be determined at isotherms of e.g. 63° C., 70° C., 80° C., 90° C. and 95° C., measuring the residual activity of samples taken from a water bath at regular intervals (e.g. every 5 or 10 min.) during a time period of 1 hour. For determining stability for the purpose of liquefaction, a pH of 5.0, a temperature of 95° C. and a total assay time of 30 to 120 minutes are used (“assay for residual activity after liquefaction”). For determining stability for the purpose of saccharification, a pH of 4.5, a temperature of 63° C. or 70° C. and a total assay time of 30 minutes are used (“assay for residual activity after saccharification”).

Alternatively, the thermostability may be expressed as a “half-time” (T_(½)), which is defined as the time, under a given set of conditions, at which the activity of the enzyme being assayed is reduced to 50% of the initial activity at the beginning of the assay. In this case, the “T_(½) assay for liquefaction” uses a pH of 5.0 and a temperature of 95° C., while the “T_(½) assay for saccharification” uses a pH of 4.5 and a temperature of 70° C. The assay is otherwise performed as described above for the respective assays for residual activity.

Activity: Somogyi-Nelson Method for Determination of Reducing Sugars

The activity of pullulanases can be measured using the Somogyi-Nelson method for the determination of reducing sugars (J. Biol. Chem. 153, 375 (1944)). This method is based on the principle that sugar reduces cupric ions to cuprous oxide, which reacts with an arsenate molybdate reagent to produce a blue colour that is measured spectrophotometrically. The solution to be measured must contain 50-600 mg of glucose per liter. The procedure for the Somogyi-Nelson method is as follows:

Sample value: Pipet 1 ml of sugar solution into a test tube. Add 1 ml of copper reagent. Stopper the test tube with a glass bead. Place the test tube in a boiling water bath for 20 minutes. Cool the test tube. Add 1 ml of Nelson's color reagent. Shake the test tube without inverting it. Add 10 ml of de-ionized water. Invert the test tube and shake vigorously. Measure the absorbance at 520 nm, inverting the test tube once immediately prior to transfer of the liquid to the cuvette.

Blank value: Same procedure as for the sample value, but with water instead of sugar solution.

Standard value: Same procedure as for the sample value.

Calculations: In the region 0-2 the absorbance is proportional to the amount of sugar. ${{mg}\quad {sugar}\text{/}l} = \frac{100\left( {{sample} - {blank}} \right)}{\left( {{standard} - {blank}} \right)}$ ${\% \quad {glucose}} = \frac{\left( {{sample} - {blank}} \right)}{100 \times \left( {{standard} - {blank}} \right)}$

Reagents

1. Somogyi's Copper Reagent

35.1 g Na₂HPO₄.2H₂O and 40.0 g potassium sodium tartrate (KNaC₄H₄O₂.4H₂O) are dissolved in 700 ml of de-ionized water. 100 ml of 1N sodium hydroxide and 80 ml of 10% cupric sulphate (CuSO₄.5H₂O) are added. 180 g of anhydrous sodium sulphate are dissolved in the mixture, and the volume is brought to 1 liter with de-ionized water.

2. Nelson's Color Reagent

50 g of ammonium molybdate are dissolved in 900 ml of de-ionized water. Then 42 ml of concentrated sulphuric acid are added, followed by 6 g of disodium hydrogen arsenate heptahydrate dissolved in 50 ml of deionized water, and the volume is brought to 1 litre with deionized water. The solution is allowed to stand for 24-48 hours at 37° C. before use and is stored in the dark in a brown glass bottle with a glass stopper.

3. Standard

100 mg of glucose (anhydrous) are dissolved in 1 liter of de-ionized water.

Alternatively, the release of reducing sugars can be measured using a 96 well plate set-up modified after Fox, J. D. & Robyt, J. F. (1991) Anal. Biochem. 195, 93-96. Assay conditions are (in brief): 1 ml substrate (e.g. 1% solution) in 50 mM citric acid pH 5 is preincubated at 60° C. A zero timepoint is taken 150 μl sample and transferred to a microtiter plate well containing 150 μl solution A+B for reducing sugar determination. The enzymatic reaction is initiated by addition of 100 μl enzyme and time points are taken at T=1, 2, 3, 4, and 5 min.

After completion of the assay, the plate is developed by incubation at 85° C. for 70 minutes and the plate is read at 540 nm.

Reagents for determination of reducing value: Solution A) and solution B (62 mg copper sulfate pentahydrate and 63 mg L-serine in 50 ml water).

Pullulanase Specificity

Methods for the determination and characterization of the profile of action and specificity of pullulanases for various substrates (e.g. amylopectin, glycogen and pullulan) are described by Kainuma et al. in Carbohydrate Research, 61 345-357 (1978). Using these methods, the relative activity of a pullulanase can be determined, and the relative activity of a pullulanase variant according to the invention compared to the relative activity of the parent pullulanase can be assessed, for example to determine whether a pullulanase variant has the desired increased specificity toward high molecular weight saccharides, such as amylopectin, compared to the parent pullulanase.

In order to determine whether the pulluanase variant possesses an increased isoamylase activity as compared to the parent pullulanse the following test may be performed (“assay for isoamylase-like activity”):

1000 mg rabbit liver glycogen is dissolved in 40 ml water to which 0.2% NaOH has been added. 800 mg NaBH₄ is added carefully under stirring. The solution is stirred for 48 hours at 25° C. after which the reaction is stopped by addition of Amberlite IR-118H (a cation exchanger which removes the boron ions and hence stops the reaction). The solution is filtered to remove the matrix and evaporated to give 10 ml. The solution is then dialyzed extensively against de-ionized water to remove residual boron ions. The parent pullulanase and the pulluanase variant are assayed according to the method of Somogyi-Nelson, using 50 mM sodium acetate, pH values of 4.5, 5.0 or 5.5 and a temperature of 60° C., with a reaction time of 10 minutes. Glucose is used as a standard, a standard curve being made from solutions containing of 0-200 mg glucose/liter.

Clearly, the higher the number of reducing ends formed during the incubation period, the higher “isoamylase activity”. The increase in the pullulanase variant's isoamylase activity is expressed as a percentage value based on the original “isoamylase activity” of the parent pullulanase.

Pullulanase Variants with Altered Stability

A variant with improved stability (typically increased thermostability) may be obtained by substitution with proline, substitution of histidine with another amino acid, introduction of a disulfide bond, removal of a deamidation site, altering a hydrogen bond contact, filling in an internal structural cavity with one or more amino acids with bulkier side groups, introduction of interdomain interactions, altering charge distribution, helix capping, or introduction of a salt bridge.

Increased Mobility Regions

The following regions have an increased mobility in the crystal structure of Promozyme®, and it is presently believed that these regions can be responsible for stability or activity of the enzyme. Improvements of the enzyme can be obtained by mutation in the below regions and positions. Introducing e.g. larger residues or residues having more atoms in the side chain could increase the stability, or e.g. introduction of residues having fewer atoms in the side chain could be important for the mobility and thus the activity profile of the enzyme. The regions can be found by analysing the B-factors taken from the pdb file, and/or from molecular dynamics calculations of the isotropic fluctuations. These can be obtained by using the program CHARMm from MSI (Molecular simulations inc.).

Thus, in order to stabilize mobile regions in the structure, a preferred variant of a parent pullulanase comprises a modification, e.g. a substitution, of an amino acid residue corresponding to one or more of the following residues of the amino acid sequence set forth in SEQ ID NO: 1:

408-429 (i.e. 408, 409, 410, 411, 412, 413, 414, 415, 416, 417, 418, 419, 420, 421, 422, 423, 424, 425, 426, 427, 428 and 429),

300-314 (i.e. 300, 301, 302, 303, 304, 305, 306, 307, 308, 309, 310, 311, 312, 313 and 314),

157-165 (i.e. 157, 158, 159, 160, 161, 162, 163, 164 and 165),

95-113 (i.e. 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108, 109, 110, 111, 112 and 113),

130-140 (i.e. 130, 131, 132, 133, 134, 135, 136, 137, 138, 139 and 140),

232-238 (i.e. 232, 233, 234, 235,236, 237 and 238),

266-272 (i.e. 266, 267, 268, 269, 270, 271 and 272),

302-308 (i.e. 302, 303, 304, 305, 306, 307 and 308),

418-428 (i.e. 418, 419, 420, 421, 422, 423, 424, 425, 426, 427 and 428),

500-507 (i.e. 500, 501, 502, 503, 504, 505, 506 and 507),

659-665 (i.e. 659, 660, 661, 662, 663, 664 and 665) and

751-755 (i.e. 751, 752, 753, 754 and 755).

Similar modifications, e.g. substitutions, may be introduced in equivalent positions of other pullulanases. Variants of particular interest have a combination of one or more of the above with any of the other modifications disclosed herein.

For example, other preferred modifications, e.g. substitutions, which are believed to stabilized mobile regions in the structure of the pullulanase from Bacillus deramificans, correspond to one or more of the following residues of the amino acid sequence set forth in SEQ ID NO: 3:

406-427 (i.e. 406, 407, 408, 409, 410, 411, 412, 413, 414, 415, 416, 417, 418, 419, 420, 421, 422, 423, 424, 425, 426 and 427),

298-312 (i.e. 298, 299, 300, 301, 302, 303, 304, 305, 306, 307, 308, 309, 310, 311 and 312),

153-161 (i.e. 153, 154, 155, 156, 157, 158, 159, 160 and 161),

91-109 (i.e. 91, 92, 93, 94, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105, 106, 107, 108 and 109),

126-136 (i.e. 126, 127, 128, 129, 130, 131, 132, 133, 134, 135 and 136),

230-236 (i.e. 230, 231, 232, 233, 234, 235 and 236),

264-270 (i.e. 264, 265, 266, 267, 268, 269 and 270),

300-306 (i.e. 300, 301, 302, 303, 304, 305 and 306),

416-426 (i.e. 416, 417, 418, 419, 420, 421, 422, 423, 424, 425 and 426),

498-505 (498, 499, 500, 501, 502, 503, 504 and 505),

656-662 (i.e. 656, 657, 658, 659, 660, 661 and 662) and

749-753 (i.e. 749, 750, 751, 752 and 753).

Furthermore, it is envisaged from the structure that deletion of certain amino acid residues will confer increased stability, such as increased thermostability, to the thus produced variant. Variants, which are believed to be of particular importance, comprises a deletion of amino acid residues corresponding to the following residues of the amino acid sequence set forth in SEQ ID NO: 1:

Deletion of the peptide fragment 158-275, such as a deletion starting from position 158, 159, 160 or 161 and ending at position 270, 271, 272, 273, 274 or 275, i.e. the longest deletion will be deletion of the peptide fragment 158-275 and the shortest deletion will be deletion of the peptide fragment 161-270.

Other deletions which are expected to confer increased stability, such as increased thermostability, to the pullulanase variant comprises a deletion of amino acid residues corresponding to the following residues of the amino acid sequence set forth in SEQ ID NO: 1:

Deletion of the peptide fragment 1-315, such as deletion of the peptide fragment 1-314, 1-313, 1-312, 1-311, 1-310, 1-309, 1-308, 1-307, 1-306, 1-305, or 1-304.

Furthermore, the following deletions are expected to confer increased stability, such as increased thermostability, to the pullulanase variant comprises a deletion of amino acid residues corresponding to the following residues of the amino acid sequence set forth in SEQ ID NO: 1:

Deletion of the peptide fragment 1-115, such as deletion of the peptide fragment 1-114, 1-113, 1-112, 1-111, 1-110, 1-109, 1-108, 1-107, 1-106 or 1-105.

Similar deletions may be introduced in equivalent positions of other pullulanases. Variants of particular interest have a combination of one or more of the above with any of the other modifications disclosed herein.

For example, it is envisaged that deletion of the below amino acid residues will confer increased stability, such as increased thermostability, to the thus produced variant of the pullulanase from Bacillus deramificans (SEQ ID NO: 3):

Deletion of the peptide fragment 154-273, such as a deletion starting from position 154, 155, 156 or 157 and ending at position 268, 269, 270, 271, 272 or 273, i.e. the longest deletion will be deletion of the peptide fragment 154-273 and the shortest deletion will be deletion of the peptide fragment 157-268.

Other deletions which are expected to confer increased stability, such as increased thermostability, to the pullulanase variant comprises a deletion of amino acid residues corresponding to the following residues of the amino acid sequence set forth in SEQ ID NO: 3:

Deletion of the peptide fragment 1-313, such as deletion of the peptide fragment 1-312, 1-311, 1-310, 1-309, 1-308, 1-307, 1-306, 1-305, 1-304, or 1-303.

Furthermore, the following deletions are expected to confer increased stability, such as increased thermostability, to the pullulanase variant comprises a deletion of amino acid residues corresponding to the following residues of the amino acid sequence set forth in SEQ ID NO: 3:

Deletion of the peptide fragment 1-111, such as deletion of the peptide fragment 1-111, 1-110, 1-109, 1-108, 1-107, 1-106, 1-105, 1-104, 1-103, 1-102 or 1-101.

Cavities and Crevices

The structure of the pullulanase contains a number of unique internal cavities, which may contain water, and a number of crevices. In order to increase the stability, preferably the thermostability, of the pullulanase it may be desirable to reduce the number or size of cavities and crevices, e.g., by introducing one or more hydrophobic contacts, preferably achieved by introducing amino acids with bulkier side chains in the vicinity or surroundings of the cavity or crevice. For instance, the amino acid residues to be modified are those which are involved in the formation of a cavity or crevice.

In order to determine which amino acid residues of a given enzyme are involved in the formation of cavities or crevices the Conolly program is normally used (B. Lee and F. M. Richards, J. Mol. Biol. 55, 379-400 (1971)). The program uses a probe with a certain radius to search the external and internal surface of the protein. The smallest crevice observable in this way has the probe radius.

To analyze the solved structure of Promozyme®, a modified version of the Connolly program included in the program of INSIGHT was used. In the first step, the water molecules and the ions were removed by unmerging these atoms from the solved structure. By using the command MOLECULE SURFACE SOLVENT the solvent accessible surface area was calculated for all atoms and residues using a probe radius of 1.4 Å, and displayed graphically together with the model of the solved structure. The internal cavities are then seen as dot surfaces with no connections to the external surface.

Suggestions for specific modifications to fill out the cavities are given below. By using the homology built structures and/or comparisons based on sequence alignment, mutations for homologous structures of pullulanases can be made.

Accordingly, in a further aspect the present invention relates to a method for constructing a variant of a parent pullulanase, the method comprising:

a) identifying an internal cavity or crevice in the three-dimensional structure of the parent pullulanase;

b) substituting at least one amino acid residue involved in the formation of a cavity or crevice with another amino acid residue which increases the hydrophobic interaction and/or fills out or reduces the size of the cavity or crevice;

c) optionally repeating steps a) and b) recursively;

d) optionally, making alterations each of which is an insertion, a deletion or a substitution of an amino acid residue at one or more positions other than b);

e) preparing the variant resulting from steps a)-d);

f) testing the stability and/or the temperature dependent activity profile of the variant; and

g) optionally repeating steps a)-f) recursively; and

h) selecting a variant having increased stability and/or an altered temperature dependent activity profile as compared to the parent pullulanase.

In a preferred embodiment of the invention the variant pullanase provided by the above method have increased thermostability as compared to the parent pullulanase. The thermostability of a given variant may be assessed as described in the above section entitled “Methods for determining stability, activity and specificity”.

It will be understood that the cavity or crevice is identified by the amino acid residues surrounding said cavity or crevice, and that modification of said amino acid residues are of importance for filling or reducing the size of the cavity or crevice. Preferably, the modification is a substitution with a bulkier amino acid residue, i.e. one with a greater side chain volume or with an increased number of atoms in the side chain. For example, all the amino acids are bulkier than Gly, whereas Tyr and Trp are bulkier than Phe. The particular amino acid residues referred to below are those which in a crystal structure have been found to flank the cavity or crevice in question.

In a preferred embodiment, the variant of a pullulanase, in order to fill, either completely or partly, cavities or crevices located internally or externally in the structure, comprises a modification, e.g. a substitution, of an amino acid residue corresponding to one or more of the following residues of the amino acid sequence set forth in SEQ ID NO: 1:

406, 394, 568, 573 576, 563, 557, 396, 392, 515, 583, 442, 792, 767, 732, 760, 783, 740, 688, 478, 534, 550, 627, 314.

In a more preferred embodiment, the variant of a pullulanse comprises one or more substitutions corresponding to the following substitutions in the amino acid sequence set forth in SEQ ID NO: 1:

G406A, P394F/W/I/L, I568L/F, Y573W, T576N/L/I, S563T, T557N, A396V/L/I, V392, N515M/L/I, V583I/F/L, D442Q, S792Y/F, V767Q/E/L/I, V732I/L, D760Q/E/F/Y, L783F/Y, L740Q, D688Y/F/E/Q/R/K, L478Q/R, L534F/Y/I, M550F/Y/I/L, L627F/Y/I, L314I.

Similar modifications, e.g. substitutions, may be introduced in equivalent positions of other pullulanases. Variants of particular interest have a combination of one or more of the above with any of the other modifications disclosed herein.

For example, the variant of a pullulanase may also comprise one or more substitutions corresponding to the following substitutions in the amino acid sequence set forth in SEQ ID NO: 3:

566, 485, 487, 437, 775, 779, 551, 428, 492, 495, 392, 621, 437+503, 674+664 and 823.

In a more preferred embodiment, the variant of a pullulanse comprises one or more substitutions corresponding to the following substitutions in the amino acid sequence set forth in SEQ ID NO: 3:

I566A, Q485H, M487L, D437H, Q775H, E779D, V551I, I428Y/F, S492F, V495I/F/Y, P392Y, L621Q, D437H+D503Y, V674+L664F and L823V.

Disulfide Bonds

A variant with improved stability (typically improved thermostability) as compared to the parent pullulanase may be obtained by introducing new interdomain and intradomain contacts, such as establishing inter- or intradomain disulfide bridges.

Accordingly, a further aspect of the present invention relates to a method for constructing a variant of a parent pullulanase, the method comprising:

a) identifying in the three-dimensional structure of the parent pullulanase two or more amino acid residues which, when substituted with cysteines, are capable of forming a disulfide bond;

b) substituting the amino acids identified in a) with cysteines;

c) optionally repeating steps a) and b) recursively;

d) optionally, making alterations each of which is an insertion, a deletion or a substitution of an amino acid residue at one or more positions other than b);

e) preparing the variant resulting from steps a)-d);

f) testing the stability of said variant; and

g) optionally repeating steps a)-f) recursively; and

h) selecting a variant having increased stability as compared to the parent pullulanase.

In a preferred embodiment of the invention the variant pullanase provided by the above method have increased thermostability as compared to the parent pullulanase. The thermostability of a given variant may be assessed as described in the above section entitled “Methods for determining stability, activity and specificity”.

In order to determine, in the three-dimensional structure of the parent pullulanase, the amino acid residues which, when substituted with cysteines, are capable of forming a disulfide bond, residues with CB atoms less than 4 Å from each other, and where the direction of the CA-CB from each residue is pointing towards the other residue are identified. Following the above-mentioned guidelines, the below amino acid residues were identified in the amino acid sequence of SEQ ID NO: 1, and it is contemplated that these residues are suitable for cystein replacement, thereby opening up the possibility of establishing one or more disulfide bridges in the variant pullulanase:

K758C+I914C, T916C+A765C, I897C+S819C, P525C+E499C, H286C+T148C.

Similar substitutions may be introduced in equivalent positions of other pullulanases. Variants of particular interest have a combination of one or more of the above with any of the other modifications disclosed herein.

For example, it is contemplated that the following residues, identified in the amino acid sequence of the pullulanase from Bacillus deramificans (SEQ ID NO: 3), are suitable for cystein replacement, thereby opening up the possibility of establishing one or more disulfide bridges in the variant pullulanase:

K756C/I912C, M914C/A763C, V895C/G817C, A523C/E497C, H284C/T144C.

Surface Charge Distribution

A variant with improved stability (typically improved thermostability) as compared to the parent pullulanase may be obtained by changing the surface charge distribution of the pullulanase. For example, when the pH is lowered to about 5 or below histidine residues typically become positively charged and, consequently, unfavorable electrostatic interactions on the protein surface may occur. By engineering the surface charge of the pullulanase one may avoid such unfavorable electrostatic interactions which in turn leads to a higher stability of the pullulanase.

Therefore, a further aspect of the present invention relates to method for constructing a variant of a parent pullulanase, the method comprising:

a) identifying, on the surface of the parent pullulanase, at least one amino acid residue selected from the group consisting of Asp, Glu, Arg, Lys and His;

b) substituting, on the surface of the parent pullulanase, at least one amino acid residue selected from the group consisting of Asp, Glu, Arg, Lys and His with an uncharged amino acid residue;

c) optionally repeating steps a) and b) recursively;

d) optionally, making alterations each of which is an insertion, a deletion or a substitution of an amino acid residue at one or more positions other than b);

e) preparing the variant resulting from steps a)-d);

f) testing the stability of said variant; and

g) optionally repeating steps a)-f) recursively; and

h) selecting a variant having increased stability as compared to the parent pullulanase.

As will be understood by the skilled person it may also, in some cases, be advantageous to substitute an uncharged amino acid residue with an amino acid residue bearing a charge or, alternatively, it may in some cases be advantageous to substitute an amino acid residue bearing a charge with an amino acid residue bearing a charge of opposite sign. Thus, the above-mentioned method may easily be employed by the skilled person also for these purposes. In the case of substituting an uncharged amino acid residue with an amino acid residue bearing a charge the above-mentioned method may be employed the only difference being steps a) and b) which will then read:

a) identifying, on the surface of the parent pullulanase, at least one uncharged amino acid residue;

b) substituting, on the surface of the parent pullulanase, at least one uncharged amino acid residue with a charged amino acid residue selected from the group consisting of Asp, Glu, Arg, Lys and His.

Also in the case of changing the sign of an amino acid residue present on the surface of the pullulanase the above method may be employed. Again, compared to the above method, the only difference being steps a) and b) which, in this case, read:

a) identifying, on the surface of the parent pullulanase, at least one charged amino acid residue selected from the group consisting of Asp, Glu, Arg, Lys and His;

b) substituting, on the surface of the parent pullulanase, at least one charged amino acid residue identified in step a) with an amino acid residue having an opposite charge.

Thus, Asp may be substituted with Arg, Lys or His; Glu may be substituted with Arg, Lys or His; Arg may be substituted with Asp or Glu; Lys may be substituted with Asp or Glu; and His may be substituted with Asp or Glu.

In a preferred embodiment of the invention the variant pullulanase provided by the above method(s) have increased thermostability as compared to the parent pullulanase. The thermostability of a given variant may be assessed as described in the above section entitled “Methods for determining stability, activity and specificity”.

In order to determine the amino acid residues of a pullulanase, which are present on the surface of the enzyme, the surface accessible area are measured using the DSSP program (Kabsch and Sander, Biopolymers (1983), 22, 2577-2637). All residues having a surface accessibilty higher than 0 is regarded a surface residue.

The amino acid residues found on the surface of Promozyme® using the above method are as follows:

E526, Q544, E760, N338, N228, N181,

and it is contemplated that the following substitutions are of particular interest:

E526H, Q544E, E760Q, N338K/R, N228DE/, N181K/R.

Similar substitutions may be introduced in equivalent positions of other pullulanases. Variants of particular interest have a combination of one or more of the above with any of the other modifications disclosed herein.

For example, the variant of a pullulanase may also comprise one or more modifications, e.g. substitutions, corresponding to the following substitutions in the amino acid sequence set forth in SEQ ID NO: 3:

444, 530, 710 and 855.

In a more preferred embodiment, the variant of a pullulanse comprises one or more substitutions corresponding to the following substitutions in the amino acid sequence set forth in SEQ ID NO: 3:

D444R/K, K530Y/F/L, N710R and T855K.

Other Modifications

Variants with improved stability, in particular variants with improved thermostability, can be obtained by improving existing or introducing new interdomain or intradomain contacts. Such improved stability can be achieved by the modifications listed below.

Thus, one preferred embodiment of the invention relates to a variant of a parent pullulanase which has an improved stability and one or more salt bridges as compared to the parent pullulanase, wherein said variant comprises a modifications, e.g. a substitution, in a position corresponding to at least one of the following sets of positions in SEQ ID NO: 1:

301, 385, 298, 299, 385 and 299+385, in particular L301R, N385R, H298R, N299R, N385D and N299R+N385D.

Similar modifications, e.g. substitutions, may be introduced in equivalent positions of other pullulanases. Variants of particular interest have a combination of one or more of the above with any of the other modifications disclosed herein.

For example, it is contemplated that the following substitutions in the pullunanase having the amino acid sequence set forth in SEQ ID NO: 3 will enhance the stability of the enzyme: T891D, S892K, T891D+S892K and N400R.

In another preferred embodiment, the variant of the pullulanase comprises a substitution corresponding to one or more of the following substitutions with proline in the amino acid sequence set forth in SEQ ID NO: 1:

G293P, K151P, K122P, N315P, N374P, N793P, A446P, G672P, G668P, T556P

In a further interesting embodiment of the invention, the variant of the pullulanase comprises a substitution corresponding to one or more of the following substitutions with proline in the amino acid sequence set forth in SEQ ID NO: 3:

D562P, G794P, G292P, D148P, N119P, D314P, N373P, N792P, G671P, G667P and T554P.

Analogously, it may be preferred that one or more histidine residue(s) present in the parent pullulanase is (are) substituted with a non-histidine residues such as Y, V I, L, F, M, E, Q, N, or D. Accordingly, in another preferred embodiment, the variant of the parent pullulanase comprises a substitution of an amino acid residue corresponding to one or more of the following residues of the amino acid sequence set forth in SEQ ID NO: 3: H422Y/F/L, H483Y/F/L, H543Y/F/L/N and H613Y/F/L.

It may be preferred that one or more asparagine or glutamine residues present in the parent pullulanase is or are substituted with a residue lacking the amide group on the side chain. Preferably, such asparagines or glutamine residues are substituted with S, T, V, L and/or F amino acid residues. Accordingly, in another preferred embodiment, the variant of the parent pullulanase comprises a modification, e.g. a substitution, of an amino acid residue corresponding to one or more of the following residues of the amino acid sequence set forth in SEQ ID NO: 1:

Q543, Q339, N337, Q380, Q353, N384, N286, N298, N227, Q227, Q210, N180, Q259, N583, N790, N793, N505, N788, N736, N684, N689 or N681, preferably Q543S/T/V/L/F, Q339S/T/V/L/F, N337S/T/V/L/F, Q380S/T/V/L/F, Q353S/T/V/L/F, N384S/T/V/L/F, N286S/T/V/L/F, N298S/T/V/L/F, N227S/T/V/L/F, Q227S/T/V/L/F, Q210S/T/V/L/F, N180S/T/V/L/F, Q259S/T/V/L/F, N583S/T/V/L/F, N790S/T/V/L/F, N793S/T/V/L/F, N505S/T/V/L/F, N788S/T/V/L/F, N736S/T/V/L/F, N684S/T/V/L/F, N689S/T/V/L/F and N681S/T/V/L/F.

The corresponding residues found in the pullulanase from Bacillus deramificans (SEQ ID NO: 3) include:

N400, N446, N504, N717, N735 and N789, preferably N400S/T/V/L/F, N446S/T/V/L/F, N504S/T/V/L/F, N717S/T/V/L/F, N735S/T/V/L/F and N789S/T/V/L/F.

Moreover, it is contemplated that modifications, e.g. substitutions, in the region linking the N2 and the A domain, as well as other regions linking other domains, will confer additional stability, such as an increased thermostability, to the enzyme. Thus, in an interesting embodiment of the invention, the pullulanase variant comprises one or more modifications, e.g. substitutions, in the domain-linking regions (e.g. the region linking the N2 and A domains).

Examples of such modifications include one or more of the following substitutions in the pullulanase from Bacillus deramificans (SEQ ID NO: 3):

111, 112,

158-160 (i.e. 158, 159 and 160),

270-274 (i.e. 270, 271, 272, 273 and 274),

302-314 (i.e. 302, 303, 304, 305, 306, 307, 308, 309, 310, 311, 312, 313 and 314) and

408-426 (i.e. 408, 409, 410, 411, 412, 413, 414, 415, 416, 417, 418, 419, 420, 421, 422, 423, 424, 425 and 426).

Examples of specific substitutions are: S111T/V/L, N112S/T/Q, S158Y/F/T, L159Y/K/R/A/S/T, G160A/S/T, D270E/S/T, L271V/I, V272I, T273N/D/E/Y/F, V274I, N302V/L/Y, N305V/L/Y, S306T/V, Q308K/R/A/S/T, Y309F, Y310E/D/Q/N/L/V/I D314A/S/T, L409N, D408S/T, A410S/T, D413R/K/S/T, A415S/T, G416S/T/V, N418A/V/S/T, S419D/N/T, K421E/Q/S/T/V/A, H422D/L/Y/F, I423L/V/S/T/N/Q, T424S/A and K426A/S/T.

Other substitutions which are considered of particular importance in SEQ ID NO:3 include D437N and D440N.

Similar modifications, e.g. substitutions, may be introduced in equivalent positions of other pullulanases. Modifications of particular interest are any combination of one or more of the above with any of the other modifications disclosed herein.

Before actually constructing a pullulanase variant to achieve any of the above objectives, it may be convenient to evaluate whether or not the contemplated amino acid modification can be accommodated into pullulanase structure, e.g. in a model of the three-dimensional structure of the parent pullulanase.

Pullulanase Variants with an Altered Substrate Specificity

One aim of the present invention is to change the degradation characteristics of a pullulanase. Thus, as Promozyme® (and pullulanases in general) exhibits a low activity towards high molecular weight branched starchy material, such as glycogen and amylopectin, it may be desirable to change this cleavage pattern, e.g. so as to obtain a higher activity against such substrates, in particular when the pullulanase is to be added during the liquefaction process.

An altered substrate specificity may be achieved by modifying the substrate binding area in a parent pullulanse.

Accordingly, the present invention also relates to a method for constructing a variant of a parent pullulanase, the method comprising:

a) identifying the substrate binding area in a model of the three-dimensional structure of the parent pullulanase;

b) modifying the substrate binding area by an amino acid substitution, deletion and/or insertion;

c) optionally repeating step b) recursively;

d) optionally, making alterations each of which is an insertion, a deletion or a substitution of an amino acid residue at one or more positions other than b),

e) preparing the variant resulting from steps a)-d);

f) testing the substrate specificity of the variant;

g) optionally repeating steps a)-f) recursively; and

h) selecting a variant having an altered substrate specificity as compared to the parent pullulanase.

The substrate binding area may easily be identified by homology to other family 13 members. The active site residues are identified by homology. The substrate-binding site is identified by the concave cavity containing the active site residues. A substrate model is docked into the cavity. A suitable substrate model is the substrate structure found in the pdb file 1BAG termed GLC. This model can be “docked” into the Promozyme X-ray structure or a modeled Pullulanase 3D structure by superimposing the active site residues in the two structures. In 1BAG one of the active site residues has been mutated into an Gln instead of the native Glu. The active site residues to be superimposed are: D269, Q208 and D176 (1BAG) with D736, E651 and D622 (Promozyme®). The superposition can be made using the program INSIGHTII.

Without being limited to any theory, it is presently believed that binding between a substrate and an enzyme is supported by favorable interactions found within a sphere 10 Å from the substrate molecule, in particular within a sphere of 6 Å from the substrate molecule. Examples of such favorable bonds are hydrogen bonds, strong electrostatic interaction and/or hydrophobic interactions. The following residues of Promozyme® (SEQ ID NO: 1), are within a distance of 10 Å from the “docked” substrate and thus believed to be involved in interactions with said substrate:

437, 439, 487, 489, 490, 514, 679, 681, 684, 685, 731, 775, 786,

494-496 (i.e. 494, 495 and 496),

505-511 (i.e. 505, 506, 507, 508, 509, 510 and 511),

551-559 (i.e. 551, 552, 553, 554, 555, 556, 557, 558 and 559),

584-590 (i.e. 584, 585, 586, 587, 588, 589 and 590),

620-626 (i.e. 620, 621, 622, 623, 624, 625, 626),

650-658 (i.e. 659, 651, 652, 653, 654, 655, 656, 657 and 568),

665-668 (i.e. 666, 667 and 668),

690-693 (i.e. 690, 691, 692 and 693),

734-738 (i.e. 734, 735, 736, 737 and 738) and

789-795 (i.e. 789, 790, 791, 792, 793, 794 and 795).

The following residues of Promozyme® are within a distance of 6 Å from the substrate and thus believed to be involved in interactions with said substrate:

489, 551, 553, 555, 556, 620, 651, 691, 692, 791, 793, 794,

506-510 (i.e. 507, 508, 509 and 510),

586-588 (i.e. 586, 587 and 588),

622-624 (i.e. 622, 623 and 624),

653-656 (i.e. 653, 654, 655 and 656) and

735-737 (i.e. 735, 736 and 737),

In a preferred embodiment of the invention, the parent pullulanase is modified in such a way that the variant pulluanase exhibits an increased isoamylase activity compared to the parent pullulanase.

When used herein, the term “increased isoamylase activity” refers in general to the fact that the pullulanase variants according to the invention exhibits a higher activity towards high molecular weight branched starchy material, such as glycogen and amylopectin as compared to the parent pullulanase, cf. above.

In an interesting embodiment of the invention the pullulanase variant has an increased isoamylase activity as defined by an increase of at least 5%, preferably of at least 10%, more preferably of at least 15%, more preferably of at least 25%, most preferably of at least 50%, in particular of at least 75%, such as of at least 100% in the number of reducing ends formed in the “assay for isoamylase-like activity” described herein, using 50 mM sodium acetate, a pH of 4.5, 5.0 or 5.5, a temperature of 60° C. and when incubated with a 10 w/v rabbit liver glycogen solution for a period of 10min.

Similar modifications may be introduced in equivalent positions of other pullulanases. Substitutions of particular interest are any combination of one or both of the above with any of the other modifications disclosed herein.

For example, the following residues of the pullulanase from Bacillus deramificans (SEQ ID NO: 3) are within a distance of 10 Å from the “docked” substrate and thus believed to be involved in interactions with said substrate:

435, 437, 485, 487, 488, 512, 677, 679, 682, 683, 729, 773, 784,

492-494 (i.e. 492, 493 and 494),

503-509 (i.e. 503, 504, 505, 506, 507, 508 and 509),

549-557 (i.e. 549, 550, 551, 552, 553, 554, 555, 556 and 557),

582-588 (i.e. 582, 583, 584, 585, 586, 587 and 588),

618-624 (i.e. 618, 619, 620, 621, 622, 623 and 624),

648-656 (648, 649, 650, 651, 652, 653, 654, 655 and 656),

663-666 (i.e. 663, 664, 665 and 666),

688-691 (i.e. 688, 689, 690 and 691),

732-736 (732, 733, 734, 735 and 736) and

787-793 (i.e. 787, 788, 879, 790, 791, 792 and 793).

The following residues of the pullulanase from Bacillus deramificans (SEQ ID NO: 3) are within a distance of 6 Å from the substrate and thus believed to be involved in interactions with said substrate:

487, 549, 551, 553, 554, 618, 649, 689, 690, 789, 791, 792,

504-508 (i.e. 504, 505, 506, 507 and 508),

584-586 (i.e. 584, 585 and 586),

620-622 (i.e. 620, 621 and 622),

651-654 (i.e. 651, 652, 653 and 654) and

733-735 (i.e. 733, 734 and 735).

Examples of specific modifications in the above-mentioned regions of Bacillus deramificans are: L621I/V, D508M/N/L/T/V, T586I/L/V, T677W/F/Y, Y729F/I/L, D679G/A/V, S732V/T/L/I, N735G/L/I/S/T/A and Δ(688-691).

Pullulanase Variants with Altered pH Dependent Activity Profile

The pH dependent activity profile can be changed by changing the pKa of residues within 15 Å, in particular by changing the pKa of residues within 10 Å, from the active site residues of the parent pullulanase. Changing the pKa of the active site residues is achieved, e.g., by changing the electrostatic interaction or hydrophobic interaction between functional groups of amino acid side chains of a given amino acid residue and its close surroundings. To obtain a higher activity at a higher pH, negatively charged residues are placed near a hydrogen donor acid, whereas positively charged residues placed near a nucleophilic acid will result in higher activity at low pH. Also, a decrease in the pKa can be obtained by reducing the accessibility of water or increasing hydrophobicity of the environment.

It is preferred that the variant in question exhibits a pH optimum which is at least about 0.5 pH units higher or lower, preferably at least about 1.0 pH units higher or lower, than the corresponding pH optimum of the parent pullulanase when tested on a suitable substrate (e.g. pullulan, amylopectin or glycogen).

Furthermore, it is particular preferred that the variant in question exhibits an increased activity in the pH range of from 4 to 5.5 as compared to the parent pullulanase when tested on a suitable substrate (e.g. pullulan, amylopectin or glycogen).

Thus, another aspect of the present invention relates to a method for constructing a variant of a parent pullulanase, the method comprising:

a) identifying an amino acid residue which is within 15 Å, in particular within 10 Å, from an active site residue of the parent pullulanase in the three-dimensional structure of said parent pullulanse, and which is involved in electrostatic or hydrophobic interactions with an active site residue;

b) substituting said amino acid residue with another amino acid residue which changes the electrostatic and/or hydrophobic surroundings of an active site residue, and which can be accommodated in the structure;

c) optionally repeating steps a) and b) recursively;

d) optionally, making alterations each of which is an insertion, a deletion or a substitution of an amino acid residue at one or more positions other than b);

e) preparing the variant resulting from steps a)-d);

f) testing the pH dependent activity of said variant; and

g) optionally repeating steps a)-f) recursively; and

h) selecting a variant having an altered pH dependent activity as compared to the parent amylase.

In general, an amino acid residue which is within 15 Å or 10 Å, respectively, from an active site residue of the parent pullulanase may be identified by using the INSIGHTII program.

In a preferred embodiment, the variant of a parent pullulanase having an altered pH dependent activity profile as compared to the parent pullulanase comprises a modification, e.g. a substitution, of an amino acid residue corresponding to one or more of the following residues of the amino acid sequence set forth in SEQ ID NO: 1 (all within 15 Å from the active site residues D736, E651, D622):

430, 433, 518, 521, 565, 599, 600, 610, 611, 635, 636, 639, 717, 760, 763, 764, 767, 817,

435-443 (i.e. 435, 436, 437, 438, 439, 440, 441, 442, and 443),

486-496 (i.e. 486, 487, 488, 489, 490, 491, 492, 493, 494, 495 and 496),

505-515 (i.e. 505, 506, 507, 508, 509, 510, 511, 512, 513, 514 and 515),

548-560 (i.e. 548, 549, 550, 551, 552, 553, 554, 555, 556, 557, 558, 559 and 560),

573-575, (i.e. 573, 574 and 575),

583-595 (i.e. 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594 and 594),

602-604 (i.e. 602, 603 and 604),

606-608 (i.e. 606-607 and 608),

616-633 (i.e. 616, 617, 618, 619, 620, 621, 622, 623, 624, 625, 626, 627, 628, 629, 630, 631, 632, and 633),

646-672 (i.e. 646, 647, 648, 649, 650, 651, 652, 653, 654, 655, 656, 657, 658, 659, 660, 661, 662, 663, 664, 665, 666, 667, 668, 669, 670, 671 and 672),

674-696 (i.e. 674, 675, 676, 677, 678, 679, 680, 681, 682, 683, 684, 685, 686, 687, 688, 689, 690, 691, 692, 693, 694, 695 and 696),

720-722 (i.e. 720, 721 and 722),

725-747 (i.e. 725, 726, 727, 728, 729, 730, 731, 732, 733, 734, 735, 736, 737, 738, 739, 740, 741, 742, 743, 744, 745, 746 and 747),

773-781 (i.e. 773, 774, 775, 776, 777, 778, 779, 780 and 781),

783-797 (i.e. 783, 784, 785, 786, 787, 788, 789, 790, 791, 792, 793, 794, 795, 796 and 797) and

799-802 (i.e. 799, 800, 801 and 802).

Within 10 Å from the active site residues D736, E651, D622:

437, 442, 492, 514, 575, 594, 603, 632, 635, 684, 688, 691, 692, 721, 727, 729, 742, 743, 775, 777, 778, 780, 784, 786, 800,

487-490 (i.e. 487, 488, 489 and 490),

507-511 (i.e. 507, 508, 509, 510 and 511),

550-557 (i.e. 550, 551, 552, 553, 554, 555, 556 and 556),

585-588 (i.e. 585, 586, 587 and 588),

590-592 (i.e. 590, 591 and 592),

619-628 (i.e. 619, 620, 621, 622, 623, 624, 625, 626, 627 and 628),

648-655 (i.e. 648, 649, 650, 651, 652, 653, 654 and 655),

665-671 (i.e. 665, 666, 667, 668, 669, 670 and 671),

676-681 (i.e. 676, 677, 678, 679, 680 and 681),

731-740 (i.e. 731, 732, 733, 734, 735, 736, 737, 738, 739 and 740) and

788-793 (i.e. 788, 789, 790, 791, 792 and 793).

Similar modifications may be introduced in equivalent positions of other pullulanases. Variants of particular interest have a combination of one or more of the above with any of the other modifications disclosed herein.

Thus, in another preferred embodiment, the variant of a parent pullulanase having an altered pH dependent activity profile as compared to the parent pullulanase comprises a modification, e.g. a substitution, of an amino acid residue corresponding to one or more of the following residues of the amino acid sequence set forth in SEQ ID NO: 3 (all within 15 Å from the active site residues D734, E649 and D620):

428, 431, 516, 519, 563, 597, 598, 608, 609, 633, 634, 637, 715, 758, 761, 762, 765, 815,

433-441 (i.e. 433, 434, 435, 436, 437, 438, 439, 440 and 441),

484-494 (i.e. 484, 485, 486, 487, 488, 489, 490, 491, 492, 493 and 494),

503-513 (i.e. 503, 504, 505, 506, 507, 508, 509, 510, 511, 512 and 513),

546-558 (546, 547, 548, 549, 550, 551, 552, 553, 554, 555, 556, 557 and 558),

571-573 (i.e. 571, 572 and 573),

581-593 (i.e. 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592 and 593),

600-602 (i.e. 600, 601 and 602),

604-606 (i.e. 604, 605 and 606),

614-631 (i.e. 614, 615, 616, 617, 618, 619, 620, 621, 622, 623, 624, 625, 626, 627, 628, 629, 630 and 631),

644-670 (i.e. 644, 645, 646, 647, 648, 649, 650, 651, 652, 653, 654, 655, 656, 657, 658, 659, 660, 661, 662, 663, 664, 665, 666, 667, 668, 669 and 670),

672-694 (i.e. 672, 673, 674, 675, 676, 677, 678, 679, 680, 681, 682, 683, 684, 685, 686, 687, 688, 689, 690,691, 692, 693 and 694),

718-720 (i.e. 718, 719 and 720),

723-745 (i.e. 723, 734, 725, 726, 727, 728, 729, 730, 731, 732, 733, 734, 735, 736, 737, 738, 739, 740, 741, 742, 743, 744 and 745),

771-779 (i.e. 771, 772, 773, 774, 775, 776, 777, 778 and 779),

781-795 (i.e. 781, 782, 783, 784, 785, 786, 787, 788, 789, 790, 791, 792, 793, 794 and 795) and

797-800 (i.e. 797, 798, 799 and 800).

Within 10 Å from the active site residues D734, E649 and D620:

435, 440, 490, 512, 573, 601, 605, 630, 669, 682, 686, 689, 690, 719, 725, 727, 740, 741, 773, 775, 776, 778, 782, 784, 798,

485-488 (i.e. 485, 486, 487 and 488),

505-509 (i.e. 505, 506, 507, 508 and 509),

548-555 (i.e. 548, 549, 550, 551, 552, 553, 554 and 555),

583-586 (i.e. 583, 584, 585 and 586),

588-590 (i.e. 588, 589 and 590),

617-626 (i.e. 616, 617, 618, 619, 620, 621, 622, 623, 624, 625 and 626),

646-653 (i.e. 646, 647, 648, 649, 650, 651, 652 and 653),

663-667 (i.e. 663, 664, 665, 666 and 667),

674-679 (i.e. 674, 675, 676, 677, 678 and 679),

729-738 (i.e. 729, 730, 731, 732, 733, 734, 735, 736, 737 and 738) and

786-791 (i.e. 786, 787, 788, 789, 790 and 791).

Specific examples of substitutions in the above-mentioned positions include D437L/I/V/F, D440L/I/V/F, M486K, M487K, D503L/I/V/F, D508N/L/T/V, T586V/I, M630H and D437L/I/V/F+D440L/I/V/F+D503L/I/V/F.

Nomenclature for Amino Acid Modifications

The nomenclature used herein for defining modifications is essentially as described in WO 92/05249. Thus, G406A indicates a substitution of the amino acid G (Gly) in position 406 with the amino acid A (Ala). G406 indicates a substitution of the amino acid G (Gly) with any other amino acid. P394F/W/I/L indicates a substitution of P394 with F, W, I or L. Δ(688-691) indicates a deletion of amino acids in positions 688-691. 412-A-413 indicates an insertion of A between amino acids 412 and 413.

When used herein, the term “modification” (of a particular amino acid residue) is intended to cover substitution and deletion (of the particular amino acid residue) as well as insertion of one or more amino acid residues after the particular amino acid residue.

Polypeptide Sequence Homology

For purposes of the present invention, the degree of homology may be suitably determined according to the method described in S. B. Needleman and C. D. Wunsch, Journal of Molecular Biology, 48, 443-45, with the following settings for polypeptide sequence comparison: GAP creation penalty of 3.0 and GAP extension penalty of 0.1. The determination may be done by means of a computer program known such as GAP provided in the UWGCG program package (Program Manual for the Wisconsin Package, Version 8, August 1994, Genetics Computer Group, 575 Science Drive, Madison, Wis., USA 53711).

Hybridization

Suitable experimental conditions for determining hybridization between a nucleotide probe and a homologous DNA or RNA sequence involves presoaking of the filter containing the DNA fragments or RNA to hybridize in 5×SSC (sodium chloride/sodium citrate, Sambrook, et al. Molecular Cloning: A Laboratory Manual, 2^(nd) Ed., Cold Spring Harbor, 1989) for 10 min, and prehybridization of the filter in a solution of 5×SSC, 5×Denhardt's solution (Sambrook, et al., 1989), 0.5% SDS and 100 μg/ml of denatured sonicated salmon sperm DNA (Sambrook, et al., 1989), followed by hybridization in the same solution containing a random-primed (A. P. Feinberg B. and Vogelstein, Anal. Biochem. 132, 6-13 (1983)), ³²P-dCTP-labeled (specific activity>1×10⁹ cpm/μg ) probe for 12 hours at ca. 45° C. The filter is then washed twice for 30 minutes in 2×SSC, 0.5% SDS at least 55° C. (low stringency), preferably at least 60° C. (medium stringency), more preferably at least 65° C. (medium/high stringency), more preferably at least 70° C. (high stringency), even more preferably at least 75° C. (very high stringency).

Molecules which hybridize to the oligonucleotide probe under these conditions are detected by exposure to x-ray film.

Methods of Preparing Pullulanase Variants According to the Invention

Cloning a DNA Sequence Encoding a Pullulanase

The DNA sequence encoding a parent pullulanase may be isolated from any cell or microorganism producing the pullulanase in question, using various methods well known in the art.

First, a genomic DNA and/or cDNA library should be constructed using chromosomal DNA or messenger RNA from the organism that produces the pullulanase to be studied. Then, if the amino acid sequence of the pullulanase is known, homologous, labelled oligonucleotide probes may be synthesised and used to identify pullulanase-encoding clones from a genomic library prepared from the organism in question. Alternatively, a labelled oligonucleotide probe containing sequences homologous to a known pullulanase gene could be used as a probe to identify pullulanase-encoding clones, using hybridization and washing conditions of lower stringency.

Alternatively, the DNA sequence encoding the enzyme may be prepared synthetically by established standard methods, e.g. the phosphoroamidite method described by S. L. Beaucage and M. H. Caruthers, Tetrahedron Letters, 22, 1859-1869 (1981) or the method described by Matthes et al. The EMBO, 3, 801-805 (1984). In the phosphoroamidite method, oligonucleotides are synthesized, e.g. in an automatic DNA synthesizer, purified, annealed, ligated and cloned in appropriate vectors.

Finally, the DNA sequence may be of mixed genomic and synthetic origin, mixed synthetic and cDNA origin or mixed genomic and cDNA origin, prepared by ligating fragments of synthetic, genomic or cDNA origin, wherein the fragments correspond to various parts of the entire DNA sequence, in accordance with techniques well known in the art. The DNA sequence may also be prepared by polymerase chain reaction (PCR) using specific primers, for instance as described in U.S. Pat. No. 4,683,202 or R. K. Saiki et al. Science, 239, 487-491(1988).

Site-directed Mutagenesis

Once a pullulanase-encoding DNA sequence has been isolated, and desirable sites for modification identified, modifications may be introduced using synthetic oligonucleotides. These oligonucleotides contain nucleotide sequences flanking the desired modification sites; mutant nucleotides are inserted during oligonucleotide synthesis. In a specific method, a single-stranded gap of DNA, bridging the pullulanase-encoding sequence, is created in a vector carrying the pullulanase gene. Then the synthetic nucleotide, bearing the desired modification, is annealed to a homologous portion of the single-stranded DNA. The remaining gap is then filled in with DNA polymerase I (Klenow fragment) and the construct is ligated using T4 ligase. A specific example of this method is described in Morinaga et al. Biotechnology 2, 639-646 (1984). U.S. Pat. No. 4,760,025 discloses the introduction of oligonucleotides encoding multiple modifications by performing minor alterations of the cassette. However, an even greater variety of modifications can be introduced at any one time by the Morinaga method because a multitude of oligonucleotides, of various lengths, can be introduced.

Another method of introducing modifications into a pullulanase-encoding DNA sequences is described in Nelson and Long Analytical Biochemistry, 180, 147-151 (1989). It involves a 3-step generation of a PCR fragment containing the desired modification introduced by using a chemically synthesized DNA strand as one of the primers in the PCR reactions. From the PCR-generated fragment, a DNA fragment carrying the modification may be isolated by cleavage with restriction endonucleases and reinserted into an expression plasmid.

Random Mutagenesis

Random mutagenesis is suitably performed either as localized or region-specific random mutagenesis in at least three parts of the gene translating to the amino acid sequence shown in question, or within the whole gene.

The random mutagenesis of a DNA sequence encoding a parent pullulanase may be conveniently performed by use of any method known in the art.

In relation to the above, a further aspect of the present invention relates to a method for generating a variant of a parent pullulanase, wherein the variant exhibits an altered property, such as increased thermostability, increased stability at low pH and at low calcium concentration, relative to the parent pullulanase, the method comprising:

(a) subjecting a DNA sequence encoding the parent pullulanase to random mutagenesis,

(b) expressing the mutated DNA sequence obtained in step (a) in a host cell, and

(c) screening for host cells expressing a pullulanase variant which has an altered property relative to the parent pullulanase.

Step (a) of the above method of the invention is preferably performed using doped primers.

For instance, the random mutagenesis may be performed by use of a suitable physical or chemical mutagenizing agent, by use of a suitable oligonucleotide, or by subjecting the DNA sequence to PCR generated mutagenesis. Furthermore, the random mutagenesis may be performed by use of any combination of these mutagenizing agents. The mutagenizing agent may, e.g., be one which induces transitions, transversions, inversions, scrambling, deletions, and/or insertions.

Examples of a physical or chemical mutagenizing agent suitable for the present purpose include ultraviolet (UV) irradiation, hydroxylamine, N-methyl-N′-nitro-N-nitrosoguanidine (MNNG), O-methyl hydroxylamine, nitrous acid, ethyl methane sulphonate (EMS), sodium bisulphite, formic acid, and nucleotide analogues. When such agents are used, the mutagenesis is typically performed by incubating the DNA sequence encoding the parent enzyme to be mutagenized in the presence of the mutagenizing agent of choice under suitable conditions for the mutagenesis to take place, and selecting for mutated DNA having the desired properties.

When the mutagenesis is performed by the use of an oligonucleotide, the oligonucleotide may be doped or spiked with the three non-parent nucleotides during the synthesis of the oligonucleotide at the positions which are to be changed. The doping or spiking may be done so that codons for unwanted amino acids are avoided. The doped or spiked oligonucleotide can be incorporated into the DNA encoding the pullulaase enzyme by any published technique, using e.g. PCR, LCR or any DNA polymerase and ligase as deemed appropriate.

Preferably, the doping is carried out using “constant random doping”, in which the percentage of wild-type and modification in each position is predefined. Furthermore, the doping may be directed toward a preference for the introduction of certain nucleotides, and thereby a preference for the introduction of one or more specific amino acid residues. The doping may be made, e.g., so as to allow for the introduction of 90% wild type and 10% modifications in each position. An additional consideration in the choice of a doping scheme is based on genetic as well as protein-structural constraints. The doping scheme may be made by using the DOPE program which, inter alia, ensures that introduction of stop codons is avoided (L. J. Jensen et al. Nucleic Acid Research, 26, 697-702 (1998).

When PCR-generated mutagenesis is used, either a chemically treated or non-treated gene encoding a parent pullulanase enzyme is subjected to PCR under conditions that increase the misincorporation of nucleotides (Deshler 1992; Leung et al., Technique, 1, 1989, pp. 11-15).

A mutator strain of E. coli (Fowler et al., Molec. Gen. Genet., 133, 1974, 179-191), S. cereviseae or any other microbial organism may be used for the random mutagenesis of the DNA encoding the pullulanase by, e.g., transforming a plasmid containing the parent enzyme into the mutator strain, growing the mutator strain with the plasmid and isolating the mutated plasmid from the mutator strain. The mutated plasmid may be subsequently transformed into the expression organism.

The DNA sequence to be mutagenized may conveniently be present in a genomic or cDNA library prepared from an organism expressing the parent pullulanase. Alternatively, the DNA sequence may be present on a suitable vector such as a plasmid or a bacteriophage, which as such may be incubated with or otherwise exposed to the mutagenising agent. The DNA to be mutagenized may also be present in a host cell either by being integrated in the genome of said cell or by being present on a vector harbored in the cell. Finally, the DNA to be mutagenized may be in isolated form. It will be understood that the DNA sequence to be subjected to random mutagenesis is preferably a cDNA or a genomic DNA sequence.

In some cases it may be convenient to amplify the mutated DNA sequence prior to performing the expression step b) or the screening step c). Such amplification may be performed in accordance with methods known in the art, the presently preferred method being PCR-generated amplification using oligonucleotide primers prepared on the basis of the DNA or amino acid sequence of the parent enzyme.

Subsequent to the incubation with or exposure to the mutagenising agent, the mutated DNA is expressed by culturing a suitable host cell carrying the DNA sequence under conditions allowing expression to take place. The host cell used for this purpose may be one which has been transformed with the mutated DNA sequence, optionally present on a vector, or one which was carried the DNA sequence encoding the parent enzyme during the mutagenesis treatment. Examples of suitable host cells are the following: gram positive bacteria such as Bacillus subtilis, Bacillus licheniformis, Bacillus lentus, Bacillus brevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus coagulans, Bacillus circulans, Bacillus lautus, Bacillus megaterium, Bacillus thuringiensis, Streptomyces lividans or Streptomyces murinus; and gram negative bacteria such as E. coli.

The mutated DNA sequence may further comprise a DNA sequence encoding functions permitting expression of the mutated DNA sequence.

Localized Random Mutagenesis

The random mutagenesis may be advantageously localized to a part of the parent pullulanase in question. This may, e.g., be advantageous when certain regions of the enzyme have been identified to be of particular importance for a given property of the enzyme, and when modified are expected to result in a variant having improved properties. Such regions may normally be identified when the tertiary structure of the parent enzyme has been elucidated and related to the function of the enzyme.

The localized, or region-specific, random mutagenesis is conveniently performed by use of PCR generated mutagenesis techniques as described above or any other suitable technique known in the art. Alternatively, the DNA sequence encoding the part of the DNA sequence to be modified may be isolated, e.g., by insertion into a suitable vector, and said part may be subsequently subjected to mutagenesis by use of any of the mutagenesis methods discussed above.

General Method for Random Mutagenesis by use of the DOPE Program

The random mutagenesis may be carried out by the following steps:

1. Select regions of interest for modification in the parent enzyme

2. Decide on mutation sites and non-mutated sites in the selected region

3. Decide on which kind of mutations should be carried out, e.g. with respect to the desired stability and/or performance of the variant to be constructed

4. Select structurally reasonable mutations

5. Adjust the residues selected by step 3 with regard to step 4.

6. Analyze by use of a suitable dope algorithm the nucleotide distribution.

7. If necessary, adjust the wanted residues to genetic code realism, e.g. taking into account constraints resulting from the genetic code, e.g. in order to avoid introduction of stop codons; the skilled person will be aware that some codon combinations cannot be used in practice and will need to be adapted

8. Make primers

9. Perform random mutagenesis by use of the primers

10. Select resulting pullulanase variants by screening for the desired improved properties.

Suitable dope algorithms for use in step 6 are well known in the art. One such algorithm is described by Tomandl, D. et al., 1997, Journal of Computer-Aided Molecular Design 11:29-38. Another algorithm is DOPE (Jensen, L J, Andersen, K V, Svendsen, A, and Kretzschmar, T (1998) Nucleic Acids Research 26:697-702).

Expression of Pullulanase Variants

The construction of the variant of interest is accomplished by cultivating a microorganism comprising a DNA sequence encoding the variant under conditions which are conducive for producing the variant, and optionally subsequently recovering the variant from the resulting culture broth. This is described in detail further below.

According to the invention, a DNA sequence encoding the variant produced by methods described above, or by any alternative methods known in the art, can be expressed, in the form of a protein or polypeptide, using an expression vector which typically includes control sequences encoding a promoter, operator, ribosome binding site, translation initiation signal, and, optionally, a repressor gene or various activator genes.

The recombinant expression vector carrying the DNA sequence encoding an pullulanase variant of the invention may be any vector which may conveniently be subjected to recombinant DNA procedures, and the choice of vector will often depend on the host cell into which it is to be introduced. Thus, the vector may be an autonomously replicating vector, i.e. a vector which exists as an extrachromosomal entity, the replication of which is independent of chromosomal replication, e.g. a plasmid, a bacteriophage or an extrachromosomal element, minichromosome or an artificial chromosome. Alternatively, the vector may be one which, when introduced into a host cell, is integrated into the host cell genome and replicated together with the chromosome(s) into which it has been integrated.

In the vector, the DNA sequence should be operably connected to a suitable promoter sequence. The promoter may be any DNA sequence which shows transcriptional activity in the host cell of choice and may be derived from genes encoding proteins either homologous or heterologous to the host cell. Examples of suitable promoters for directing the transcription of the DNA sequence encoding a pullulanase variant of the invention, especially in a bacterial host, are the promoter of the lac operon of E. coli, the Streptomyces coelicolor agarase gene dagA promoters, the promoters of the Bacillus licheniformis α-amylase gene (amyL), the promoters of the Bacillus stearothermophilus maltogenic amylase gene (amyM), the promoters of the Bacillus amyloliquefaciens α-amylase (amyQ), the promoters of the Bacillus subtilis xyIA and xyIB genes, etc. For transcription in a fungal host, examples of useful promoters are those derived from the gene encoding A. oryzae TAKA amylase, Rhizomucor miehei aspartic proteinase, A. niger neutral α-amylase, A. niger acid stable α-amylase, A. niger glucoamylase, Rhizomucor miehei lipase, A. oryzae alkaline protease, A. oryzae triose phosphate isomerase or A. nidulans acetamidase.

The expression vector of the invention may also comprise a suitable transcription terminator and, in eukaryotes, polyadenylation sequences operably connected to the DNA sequence encoding the pullulanase variant of the invention. Termination and polyadenylation sequences may suitably be derived from the same sources as the promoter.

The vector may further comprise a DNA sequence enabling the vector to replicate in the host cell in question. Examples of such sequences are the origins of replication of plasmids pUC19, pACYC177, pUB110, pE194, pAMB1 and pIJ702.

The vector may also comprise a selectable marker, e.g. a gene the product of which complements a defect in the host cell, such as the dal genes from B. subtilis or B. licheniformis, or one which confers antibiotic resistance such as ampicillin, kanamycin, chloramphenicol or tetracycline resistance. Furthermore, the vector may comprise Aspergillus selection markers such as amdS, argB, niaD and sC, a marker giving rise to hygromycin resistance, or the selection may be accomplished by co-transformation, e.g. as described in WO 91/17243.

While intracellular expression may be advantageous in some respects, e.g. when using certain bacteria as host cells, it is generally preferred that the expression is extracellular. In general, the Bacillus α-amylases mentioned herein comprise a pre-region permitting secretion of the expressed protease into the culture medium. If desirable, this preregion may be replaced by a different preregion or signal sequence, conveniently accomplished by substitution of the DNA sequences encoding the respective preregions.

The procedures used to ligate the DNA construct of the invention encoding the pullulanase variant, the promoter, terminator and other elements, respectively, and to insert them into suitable vectors containing the information necessary for replication, are well known to persons skilled in the art (cf., for instance, Sambrook et al. Molecular Cloning: A Laboratory Manual, 2^(nd) Ed., Cold Spring Harbor, 1989).

The cell of the invention, either comprising a DNA construct or an expression vector of the invention as defined above, is advantageously used as a host cell in the recombinant production of a pullulanase variant of the invention. The cell may be transformed with the DNA construct of the invention encoding the variant, conveniently by integrating the DNA construct (in one or more copies) in the host chromosome. This integration is generally considered to be an advantage as the DNA sequence is more likely to be stably maintained in the cell. Integration of the DNA constructs into the host chromosome may be performed according to conventional methods, e.g. by homologous or heterologous recombination. Alternatively, the cell may be transformed with an expression vector as described above in connection with the different types of host cells.

The cell of the invention may be a cell of a higher organism such as a mammal or an insect, but is preferably a microbial cell, e.g. a bacterial or a fungal (including yeast) cell.

Examples of suitable bacteria are gram positive bacteria such as Bacillus subtilis, Bacillus licheniformis, Bacillus lentus, Bacillus brevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus coagulans, Bacillus circulans, Bacillus lautus, Bacillus megaterium, Bacillus thuringiensis, or Streptomyces lividans or Streptomyces murinus, or gram negative bacteria such as E.coli. The transformation of the bacteria may, for instance, be effected by protoplast transformation or by using competent cells in a manner known per se.

The yeast organism may favourably be selected from a species of Saccharomyces or Schizosaccharomyces, e.g. Saccharomyces cerevisiae. The filamentous fungus may advantageously belong to a species of Aspergillus, e.g. Aspergillus oryzae or Aspergillus niger. Fungal cells may be transformed by a process involving protoplast formation and transformation of the protoplasts followed by regeneration of the cell wall in a manner known per se. A suitable procedure for transformation of Aspergillus host cells is described in EP 238 023.

In a yet further aspect, the present invention relates to a method for producing a pullulanase variant of the invention, the method comprising: cultivating a host cell as described above under conditions conducive to the production of the variant and recovering the variant from the cells and/or culture medium.

The medium used to cultivate the cells may be any conventional medium suitable for growing the host cell in question and obtaining expression of the pullulanase variant of the invention. Suitable media are available from commercial suppliers or may be prepared according to published recipes (e.g. as described in catalogues of the American Type Culture Collection).

The pullulanase variant secreted from the host cells may conveniently be recovered from the culture medium by well-known procedures, including separating the cells from the medium by centrifugation or filtration, and precipitating proteinaceous components of the medium by means of a salt such as ammonium sulfate, followed by the use of chromatographic procedures such as ion exchange chromatography, affinity chromatography, or the like.

Testing of Pullulanase

Pullulanase variants produced by any of the methods described above may be tested, either prior to or after purification, for pullulanase activity in a screening assay which measures the ability of the variant to degrade pullulan or, in case it is desired to screen for an increased isoamylases activity, the ability of the variant to degrade amylopectin. The screening in step 10 in the above-mentioned random mutagenesis method of the invention may be conveniently performed by use of a filter assay based on the following procedure: A microorganism capable of expressing the mutated pullulanase of interest is incubated on a suitable medium and under suitable conditions for secretion of the enzyme, the medium being covered with two filters comprising a protein-binding filter placed under a second filter exhibiting a low protein binding capability. The microorganism is grown on the second, top filter. Subsequent to the incubation, the bottom protein-binding filter comprising enzymes secreted from the microorganism is separated from the second filter comprising the microorganism. The protein-binding filter is then subjected to screening for the desired enzymatic activity, and the corresponding microbial colonies present on the second filter are identified. The first filter used for binding the enzymatic activity may be any protein-binding filter, e.g., nylon or nitrocellulose. The second filter carrying the colonies of the expression organism may be any filter that has no or low affinity for binding proteins, e.g., cellulose acetate or Durapore®.

Screening consists of treating the first filter to which the secreted protein is bound with a substrate that allows detection of the activity. The enzymatic activity may be detected by a dye, fluorescence, precipitation, pH indicator, IR-absorbance or any other known technique for detection of enzymatic activity. The detecting compound may be immobilized by any immobilizing agent e.g. agarose, agar, gelatine, polyacrylamide, starch, filter paper, cloth; or any combination of immobilizing agents. For example, isoamylase activity can be detected by Cibacron Red labelled amylopectin, which is immobilized in agarose. isoamylase activity on this substrate produces zones on the plate with reduced red color intensity (clearing zones).

To screen for variants with increased stability, the filter with bound pullulanase variants can be pretreated prior to the detection step described above to inactivate variants that do not have improved stability relative to the parent pullulanase. This inactivation step may consist of, but is not limited to, incubation at elevated temperatures in the presence of a buffered solution at any pH from pH 2 to 12, and/or in a buffer containing another compound known or thought to contribute to altered stability e.g., surfactants, EDTA, EGTA, wheat flour components, or any other relevant additives. Filters so treated for a specified time are then rinsed briefly in deionized water and placed on plates for activity detection as described above. The conditions are chosen such that stabilized variants show increased enzymatic activity relative to the parent after incubation on the detection media.

To screen for variants with altered thermostability, filters with bound variants are incubated in buffer at a given pH (e.g., in the range from pH 2-12) at an elevated temperature (e.g., in the range from 50°-110° C.) for a time period (e.g., from 1-20 minutes) to inactivate nearly all of the parent pullulanase, rinsed in water, then placed directly on a detection plate containing immobilized Cibacron Blue labeled pullulan and incubated until activity is detectable. As will be understood, thermostability and increased isoamylase activity may be tested simultaneously by using a detection plate containing immobilized Cibacron Red labeled amylopectin and incubate until activity is detectable. Moreover, pH dependent stability can be screened for by adjusting the pH of the buffer in the above inactivation step such that the parent pullulanase is inactivated, thereby allowing detection of only those variants with increased stability at the pH in question. To screen for variants with increased calcium-dependent stability, calcium chelators, such as ethylene glycol-bis(β-aminoethyl ether) N,N,N′,N′-tetraacetic acid (EGTA), is added to the inactivation buffer at a concentration such that the parent pullulanase is inactivated under conditions further defined, such as buffer pH, temperature or a specified length of incubation.

The variants of the invention may be suitably tested by assaying the pullulan- or amylopectin-degrading activity of the variant, for instance by growing host cells transformed with a DNA sequence encoding a variant on a starch-containing agarose plate and identifying pullulan- and/or amylopectin-degrading host cells as described above. Further testing in regard to altered properties, including specific activity, substrate specificity, cleavage pattern, thermoactivation, thermostability, pH dependent activity or optimum, pH dependent stability, temperature dependent activity or optimum, transglycosylation activity, stability, and any other parameter of interest, may be performed on purified variants in accordance with methods known in the art as described below.

The invention is further illustrated with reference to the following examples which are not intended to be in any way limiting to the scope of the invention as claimed.

EXAMPLES

Determination of Pullulanase Activity

Endo-pullulanase activity in NPUN is measured relative to a Novo Nordisk pullulanase standard. One pullulanase unit (NPUN) is defined as the amount of enzyme which releases 1 mmol glucose per minute under the standard conditions (0.7% red pullulan, pH 5, 40° C., 20 minutes). The activity is measured in NPUN/ml using red pullulan.

1 ml diluted sample or standard is incubated at 40° C. for 2 minutes. 0.5 ml 2% red pullulan, 0.5 M KCl, 50 mM citric acid, pH 5 are added and mixed. The tubes are incubated at 40° C. for 20 minutes and stopped by adding 2.5 ml 80% ethanol. The tubes are left standing at room temperature for 10-60 minutes followed by centrifugation 10 minutes at 4000 rpm. OD of the supernatants is then measured at 510 nm and the activity calculated using a standard curve.

Expression of Pullulanase from Bacillus deramificans

The pullulanase from Bacillus deramificans (SEQ ID NO: 3) is expressed in B. subtilis from a plasmid denoted pCA36. This plasmid contains the complete gene encoding the pullulanase, the expression of which is directed by the promoter from Bacillus amyloliquefaciens α-amylase. Further, the plasmid contains the origin of replication, oriT, from plasmid pUB110 and the cat gene from plasmid pC194 conferring resistance towards chloramphenicol. PCA36 is shown in FIG. 1.

Example 1

Construction of Bacillus deramificans D620A Variant

Gene specific primer 132011 and mutagenic primer 132012 are used to amplify by PCR an approximately 410 bp DNA fragment from the pCA36 plasmid.

The 410 bp fragment is purified from an agarose gel and used as a Mega-primer together with primer 136054 in a second PCR carried out on the same template.

The resulting approximately 1110 bp fragment is digested with restriction enzymes BsiW I and Mlu I and the resulting approximately 330 bp DNA fragment is purified and ligated with the pCA36 plasmid digested with the same enzymes. Competent Bacillus subtilis SHA273 (amylase and protease low) cells are transformed with the ligation and chlorampenicol resistant transformants are checked by colony PCR.

The mutagenesis primer 132012 introduced the D620A substitution (written in bold in the primer seq.) and introduced simultaneously a Bgl I restriction site (underlined in the primer seq.), which facilitates easy pinpointing of mutants.

Finally, DNA sequencing was carried out to verify the presence of the correct mutations on the plasmid.

Primer 132011: 5′ CGCTTCGGAATCATTAGGATTGC 3′ (SEQ ID NO:7)

Primer 132012: 5′ GCTTCCGTTTTGCCTTAATGGCGCTGC 3′ (SEQ ID NO:8)

Primer 136054: 5′ GGCCAAGGCTCTACCCGAACGGC 3′ (SEQ ID NO:9)

Example 2

Construction of Bacillus deramificans E649A Variant

This variant constructed as described in Example 1, except that mutagenic primer 132013 is used. The mutagenesis primer 132013 introduced the E649A substitution (written in bold in the primer seq.) and a Nar I restriction site(underlined in the primer seq.), which facilitates easy pinpointing of mutants.

Primer 132013: 5′ GCACTTTACGGGGCGCCATGGACGGG 3′ (SEQ ID NO: 10)

APPENDIX 1   1 N PRO A 112 80.159 5.264 −8.274 1.00 42.79   2 CA PRO A 112 79.045 4.605 −7.604 1.00 41.43   3 C PRO A 112 79.488 3.326 −6.903 1.00 39.90   4 O PRO A 112 80.510 2.695 −7.236 1.00 39.13   5 CB PRO A 112 78.020 4.300 −8.676 1.00 41.58   6 CG PRO A 112 78.845 4.164 −9.902 1.00 42.58   7 CD PRO A 112 79.947 5.166 −9.749 1.00 43.50   8 N SER A 113 78.659 2.987 −5.901 1.00 36.72   9 CA SER A 113 79.034 1.812 −5.120 1.00 35.45  10 C SER A 113 77.884 0.992 −4.544 1.00 33.99  11 O SER A 113 76.732 1.456 −4.501 1.00 33.34  12 CB SER A 113 79.793 2.427 −3.932 1.00 36.77  13 OG SER A 113 78.763 3.023 −3.107 1.00 37.94  14 N VAL A 114 78.232 −0.222 −4.096 1.00 30.90  15 CA VAL A 114 77.141 −0.914 −3.375 1.00 31.03  16 C VAL A 114 77.274 −0.292 −1.972 1.00 29.16  17 O VAL A 114 78.389 −0.274 −1.420 1.00 31.09  18 CB VAL A 114 77.417 −2.419 −3.553 1.00 31.41  19 CG1 VAL A 114 76.525 −3.253 −2.635 1.00 30.36  20 CG2 VAL A 114 77.488 −3.080 −4.917 1.00 30.56  21 N SER A 115 76.266 0.401 −1.479 1.00 27.09  22 CA SER A 115 76.390 1.084 −0.183 1.00 25.38  23 C SER A 115 76.091 0.149 0.997 1.00 24.90  24 O SER A 115 76.347 0.637 2.117 1.00 24.00  25 CB SER A 115 75.558 2.373 −0.187 1.00 22.77  26 OG SER A 115 74.201 2.001 −0.328 1.00 22.64  27 N ASN A 116 75.460 −0.989 0.840 1.00 23.19  28 CA ASN A 116 75.223 −1.897 1.968 1.00 22.52  29 C ASN A 116 74.830 −3.257 1.420 1.00 21.30  30 O ASN A 116 74.230 −3.250 0.354 1.00 20.56  31 CB ASN A 116 74.117 −1.373 2.885 1.00 23.16  32 CG ASN A 116 74.004 −2.136 4.191 1.00 21.84  33 OD1 ASN A 116 74.777 −1.866 5.122 1.00 20.82  34 ND2 ASN A 116 73.090 −3.083 4.280 1.00 20.73  35 N ALA A 117 75.230 −4.313 2.098 1.00 19.74  36 CA ALA A 117 74.843 −5.672 1.740 1.00 19.18  37 C ALA A 117 74.602 −6.504 3.002 1.00 20.75  38 O ALA A 117 75.366 −6.467 3.957 1.00 21.21  39 CB ALA A 117 75.831 −6.457 0.873 1.00 17.81  40 N TYR A 118 73.479 −7.242 2.937 1.00 19.90  41 CA TYR A 118 73.080 −8.099 4.042 1.00 20.50  42 C TYR A 118 72.917 −9.549 3.578 1.00 19.96  43 O TYR A 118 72.422 −9.839 2.494 1.00 22.33  44 CB TYR A 118 71.739 −7.589 4.569 1.00 20.09  45 CG TYR A 118 71.932 −6.424 5.476 1.00 18.77  46 CD1 TYR A 118 73.008 −6.394 6.361 1.00 18.02  47 CD2 TYR A 118 70.931 −5.460 5.586 1.00 17.79  48 CE1 TYR A 118 73.073 −5.426 7.355 1.00 17.37  49 CE2 TYR A 118 70.987 −4.499 6.586 1.00 17.81  50 CZ TYR A 118 72.050 −4.480 7.470 1.00 17.70  51 OH TYR A 118 72.116 −3.520 8.458 1.00 16.31  52 N LEU A 119 73.396 −10.483 4.417 1.00 17.54  53 CA LEU A 119 73.089 −11.871 4.133 1.00 17.55  54 C LEU A 119 71.822 −12.293 4.863 1.00 17.58  55 O LEU A 119 71.801 −12.501 6.070 1.00 16.85  56 CB LEU A 119 74.257 −12.745 4.571 1.00 17.57  57 CG LEU A 119 74.043 −14.215 4.193 1.00 20.46  58 CD1 LEU A 119 73.879 −14.416 2.682 1.00 20.82  59 CD2 LEU A 119 75.196 −15.116 4.624 1.00 21.33  60 N ASP A 120 70.677 −12.315 4.183 1.00 17.72  61 CA ASP A 120 69.372 −12.510 4.811 1.00 16.35  62 C ASP A 120 68.815 −13.933 4.760 1.00 17.71  63 O ASP A 120 67.794 −14.173 5.449 1.00 16.09  64 CB ASP A 120 68.314 −11.512 4.346 1.00 17.88  65 CG ASP A 120 68.469 −10.114 4.912 1.00 18.37  66 OD1 ASP A 120 69.040 −9.909 5.994 1.00 17.74  67 OD2 ASP A 120 68.000 −9.132 4.295 1.00 21.04  68 N ASP A 121 69.459 −14.847 4.069 1.00 16.19  69 CA ASP A 121 69.009 −16.253 4.082 1.00 19.25  70 C ASP A 121 70.291 −17.036 3.749 1.00 18.78  71 O ASP A 121 71.251 −16.347 3.404 1.00 16.73  72 CB ASP A 121 67.838 −16.599 3.188 1.00 18.82  73 CG ASP A 121 67.081 −17.860 3.551 1.00 21.17  74 OD1 ASP A 121 65.897 −17.937 3.106 1.00 21.16  75 OD2 ASP A 121 67.552 −18.838 4.190 1.00 19.81  76 N GLU A 122 70.312 −18.367 3.847 1.00 20.61  77 CA GLU A 122 71.613 −19.020 3.562 1.00 23.88  78 C GLU A 122 72.181 −18.700 2.193 1.00 21.23  79 O GLU A 122 73.415 −18.680 2.060 1.00 20.25  80 CB GLU A 122 71.517 −20.512 3.825 1.00 26.85  81 CG GLU A 122 70.813 −21.249 2.697 1.00 31.98  82 CD GLU A 122 70.644 −22.717 3.015 1.00 35.92  83 OE1 GLU A 122 71.596 −23.371 3.499 1.00 38.33  84 OE2 GLU A 122 69.534 −23.235 2.779 1.00 40.26  85 N LYS A 123 71.395 −18.480 1.147 1.00 21.26  86 CA LYS A 123 71.909 −18.121 −0.170 1.00 22.79  87 C LYS A 123 71.247 −16.879 −0.755 1.00 22.17  88 O LYS A 123 71.137 −16.788 −1.992 1.00 22.07  89 CB LYS A 123 71.655 −19.303 −1.115 1.00 24.69  90 CG LYS A 123 72.497 −20.528 −0.798 1.00 27.82  91 CD LYS A 123 71.837 −21.782 −1.305 1.00 30.95  92 CE LYS A 123 72.745 −22.985 −1.438 1.00 33.61  93 NZ LYS A 123 71.885 −24.227 −1.408 1.00 38.51  94 N THR A 124 70.862 −15.914 0.062 1.00 18.31  95 CA THR A 124 70.223 −14.686 −0.397 1.00 19.05  96 C THR A 124 70.918 −13.424 0.117 1.00 19.03  97 O THR A 124 71.042 −13.313 1.342 1.00 18.19  98 CB THR A 124 68.759 −14.614 0.096 1.00 19.49  99 OG1 THR A 124 68.093 −15.853 −0.273 1.00 21.02  100 CG2 THR A 124 67.958 −13.436 −0.417 1.00 17.02  101 N VAL A 125 71.314 −12.463 −0.717 1.00 18.66  102 CA VAL A 125 71.852 −11.220 −0.221 1.00 20.11  103 C VAL A 125 70.971 −10.047 −0.698 1.00 20.51  104 O VAL A 125 70.485 −10.031 −1.819 1.00 21.45  105 CB VAL A 125 73.343 −10.945 −0.302 1.00 22.08  106 CG1 VAL A 125 74.227 −12.123 −0.759 1.00 21.11  107 CG2 VAL A 125 73.756 −9.615 −0.901 1.00 19.94  108 N LEU A 126 70.757 −9.068 0.176 1.00 19.28  109 CA LEU A 126 69.973 −7.883 −0.113 1.00 19.43  110 C LEU A 126 70.940 −6.717 −0.189 1.00 20.40  111 O LEU A 126 71.583 −6.433 0.840 1.00 17.65  112 CB LEU A 126 68.962 −7.679 1.033 1.00 19.40  113 CG LEU A 126 68.214 −6.352 0.939 1.00 21.05  114 CD1 LEU A 126 67.147 −6.379 −0.146 1.00 17.96  115 CD2 LEU A 126 67.643 −5.843 2.254 1.00 18.86  116 N ALA A 127 71.204 −6.161 −1.360 1.00 20.21  117 CA ALA A 127 72.232 −5.138 −1.506 1.00 23.09  118 C ALA A 127 71.665 −3.800 −1.965 1.00 24.49  119 O ALA A 127 70.837 −3.785 −2.898 1.00 24.26  120 CB ALA A 127 73.302 −5.630 −2.495 1.00 22.46  121 N LYS A 128 72.080 −2.709 −1.336 1.00 25.87  122 CA LYS A 128 71.568 −1.383 −1.764 1.00 27.63  123 C LYS A 128 72.616 −0.764 −2.712 1.00 27.55  124 O LYS A 128 73.804 −0.895 −2.438 1.00 24.66  125 CB LYS A 128 71.296 −0.455 −0.592 1.00 26.80  126 CG LYS A 128 70.839 0.946 −0.922 1.00 27.35  127 CD LYS A 128 69.376 1.128 −1.234 1.00 26.29  128 CE LYS A 128 69.084 2.556 −1.653 1.00 27.49  129 NZ LYS A 128 69.797 3.575 −0.886 1.00 29.77  130 N LEU A 129 72.178 −0.105 −3.777 1.00 29.12  131 CA LEU A 129 73.115 0.531 −4.714 1.00 29.81  132 C LEU A 129 73.067 2.052 −4.625 1.00 30.79  133 O LEU A 129 71.997 2.621 −4.412 1.00 29.69  134 CB LEU A 129 72.693 0.064 −6.092 1.00 29.38  135 CG LEU A 129 72.670 −1.425 −6.455 1.00 29.89  136 CD1 LEU A 129 72.293 −1.585 −7.931 1.00 30.38  137 CD2 LEU A 129 74.009 −2.112 −6.236 1.00 28.39  138 N SER A 130 74.162 2.782 −4.801 1.00 32.54  139 CA SER A 130 74.086 4.228 −4.641 1.00 34.33  140 C SER A 130 73.299 4.884 −5.773 1.00 36.79  141 O SER A 130 73.009 6.074 −5.768 1.00 37.29  142 CB SER A 130 75.512 4.788 −4.600 1.00 33.55  143 OG SER A 130 76.227 4.352 −5.759 1.00 34.68  144 N MET A 131 72.979 4.059 −6.795 1.00 37.15  145 CA MET A 131 72.225 4.581 −7.925 1.00 39.70  146 C MET A 131 71.602 3.473 −8.788 1.00 38.38  147 O MET A 131 72.036 2.331 −8.785 1.00 36.96  148 CB MET A 131 73.143 5.484 −8.760 1.00 42.16  149 CG MET A 131 74.218 4.719 −9.540 1.00 44.07  150 SD MET A 131 74.661 5.555 −11.071 1.00 48.37  151 CE MET A 131 76.298 6.126 −10.590 1.00 45.57  152 N PRO A 132 70.445 3.644 −9.407 1.00 38.54  153 CA PRO A 132 69.715 2.529 −9.985 1.00 38.36  154 C PRO A 132 70.487 1.983 −11.172 1.00 39.15  155 O PRO A 132 71.420 2.615 −11.696 1.00 39.25  156 CB PRO A 132 68.348 3.076 −10.341 1.00 39.31  157 CG PRO A 132 68.452 4.555 −10.271 1.00 39.22  158 CD PRO A 132 69.703 4.916 −9.513 1.00 39.47  159 N MET A 133 70.115 0.773 −11.554 1.00 38.46  160 CA MET A 133 70.680 0.062 −12.683 1.00 37.37  161 C MET A 133 69.465 −0.615 −13.315 1.00 38.14  162 O MET A 133 68.403 −0.628 −12.657 1.00 38.27  163 CB MET A 133 71.752 −0.962 −12.320 1.00 36.83  164 CG MET A 133 71.329 −2.070 −11.385 1.00 35.87  165 SD MET A 133 72.282 −3.590 −11.397 1.00 36.52  166 CE MET A 133 73.976 −3.108 −11.265 1.00 34.78  167 N THR A 134 69.598 −1.070 −14.564 1.00 38.11  168 CA THR A 134 68.453 −1.786 −15.145 1.00 37.87  169 C THR A 134 69.034 −3.203 −15.229 1.00 38.03  170 O THR A 134 70.166 −3.414 −15.685 1.00 35.72  171 CB THR A 134 67.747 −1.212 −16.362 1.00 39.56  172 OG1 THR A 134 68.167 −1.836 −17.592 1.00 40.70  173 CG2 THR A 134 67.867 0.296 −16.567 1.00 38.10  174 N LEU A 135 68.277 −4.155 −14.682 1.00 38.56  175 CA LEU A 135 68.779 −5.531 −14.645 1.00 38.93  176 C LEU A 135 68.807 −6.218 −1.003 1.00 40.69  177 O LEU A 135 67.927 −6.085 −1.837 1.00 40.85  178 CB LEU A 135 67.967 −6.330 −13.628 1.00 36.13  179 CG LEU A 135 67.915 −5.773 −12.197 1.00 33.81  180 CD1 LEU A 135 66.758 −6.408 −11.456 1.00 33.44  181 CD2 LEU A 135 69.218 −5.959 −11.427 1.00 31.63  182 N ALA A 136 69.851 −7.010 −16.203 1.00 42.89  183 CA ALA A 136 69.985 −7.876 −17.381 1.00 43.50  184 C ALA A 136 69.636 −9.277 −16.895 1.00 44.87  185 O ALA A 136 69.205 −9.395 −15.735 1.00 44.05  186 CB ALA A 136 71.376 −7.739 −17.952 1.00 42.02  187 N ASP A 137 69.783 −10.304 −17.719 1.00 45.61  188 CA ASP A 137 69.441 −11.652 −17.302 1.00 45.76  189 C ASP A 137 70.415 −12.326 −16.333 1.00 42.62  190 O ASP A 137 71.558 −11.918 −16.176 1.00 41.07  191 CB ASP A 137 69.547 −12.644 −18.479 1.00 49.36  192 CG ASP A 137 68.263 −12.743 −19.277 1.00 52.75  193 OD1 ASP A 137 68.067 −11.851 −20.128 1.00 54.23  194 OD2 ASP A 137 67.474 −13.687 −19.039 1.00 54.86  195 N ALA A 138 69.898 −13.417 −15.742 1.00 40.77  196 CA ALA A 138 70.755 −14.138 −14.777 1.00 39.52  197 C ALA A 138 71.379 −13.240 −13.678 1.00 37.28  198 O ALA A 138 70.708 −12.438 −13.041 1.00 35.69  199 CB ALA A 138 71.862 −14.845 −15.560 1.00 38.20  200 N ALA A 139 72.686 −13.513 −13.520 1.00 34.74  201 CA ALA A 139 73.425 −12.724 −12.554 1.00 35.56  202 C ALA A 139 73.532 −11.183 −12.677 1.00 35.73  203 O ALA A 139 73.900 −10.477 −11.730 1.00 35.31  204 CB ALA A 139 74.919 −13.209 −12.589 1.00 34.52  205 N SER A 140 73.342 −10.684 −13.897 1.00 33.61  206 CA SER A 140 73.339 −9.259 −14.191 1.00 31.82  207 C SER A 140 74.597 −8.519 −13.797 1.00 30.11  208 O SER A 140 74.538 −7.393 −13.302 1.00 28.60  209 CB SER A 140 72.075 −8.690 −13.546 1.00 32.25  210 OG SER A 140 71.767 −7.352 −13.873 1.00 33.30  211 N GLY A 141 75.769 −9.122 −13.958 1.00 30.48  212 CA GLY A 141 77.065 −8.569 −13.643 1.00 29.15  213 C GLY A 141 77.524 −8.599 −12.198 1.00 30.03  214 O GLY A 141 78.613 −8.120 −11.877 1.00 29.74  215 N PHE A 142 76.701 −9.126 −11.278 1.00 29.58  216 CA PHE A 142 77.047 −9.134 −9.867 1.00 27.65  217 C PHE A 142 78.017 −10.281 −9.612 1.00 28.38  218 O PHE A 142 77.839 −11.354 −10.191 1.00 28.16  219 CB PHE A 142 75.796 −9.311 −8.977 1.00 25.35  220 CG PHE A 142 74.956 −8.071 −8.790 1.00 24.90  221 CD1 PHE A 142 75.222 −7.188 −7.760 1.00 25.18  222 CD2 PHE A 142 73.892 −7.778 −9.620 1.00 24.79  223 CE1 PHE A 142 74.496 −6.026 −7.579 1.00 25.01  224 CE2 PHE A 142 73.144 −6.628 −9.448 1.00 25.31  225 CZ PHE A 142 73.437 −5.749 −8.425 1.00 24.62  226 N THR A 143 78.971 −10.095 −8.696 1.00 28.09  227 CA THR A 143 79.811 −11.224 −8.292 1.00 29.96  228 C THR A 143 79.908 −11.299 −6.764 1.00 28.75  229 O THR A 143 79.791 −10.273 −6.092 1.00 30.13  230 CB THR A 143 81.234 −11.093 −8.857 1.00 30.83  231 OG1 THR A 143 81.625 −9.746 −8.536 1.00 32.43  232 CG2 THR A 143 81.348 −11.292 −10.365 1.00 31.64  233 N VAL A 144 80.192 −12.468 −6.219 1.00 27.73  234 CA VAL A 144 80.403 −12.603 −4.774 1.00 26.92  235 C VAL A 144 81.718 −13.339 −4.556 1.00 27.73  236 O VAL A 144 81.994 −14.337 −5.233 1.00 27.48  237 CB VAL A 144 79.255 −13.330 −4.060 1.00 24.80  238 CG1 VAL A 144 79.645 −13.759 −2.633 1.00 24.36  239 CG2 VAL A 144 78.034 −12.421 −3.949 1.00 24.13  240 N ILE A 145 82.561 −12.879 −3.637 1.00 28.05  241 CA ILE A 145 83.791 −13.551 −3.267 1.00 28.41  242 C ILE A 145 83.948 −13.647 −1.740 1.00 28.01  243 O ILE A 145 83.742 −12.756 −0.920 1.00 25.69  244 CB ILE A 145 85.080 −12.944 −3.871 1.00 31.57  245 CG1 ILE A 145 85.020 −12.914 −5.399 1.00 34.81  246 CG2 ILE A 145 86.300 −13.815 −3.542 1.00 31.61  247 CD1 ILE A 145 85.691 −11.801 −6.162 0.00 38.05  248 N ASP A 146 84.373 −14.837 −1.350 1.00 25.58  249 CA ASP A 146 84.778 −15.165 0.006 1.00 28.42  250 C ASP A 146 86.263 −14.824 0.057 1.00 28.22  251 O ASP A 146 87.082 −15.643 −0.371 1.00 27.06  252 CB ASP A 146 84.462 −16.636 0.239 1.00 26.87  253 CG ASP A 146 84.854 −17.200 1.576 1.00 28.99  254 OD1 ASP A 146 85.512 −16.536 2.398 1.00 27.91  255 OD2 ASP A 146 84.521 −18.391 1.822 1.00 28.00  256 N LYS A 147 86.657 −13.694 0.591 1.00 29.63  257 CA LYS A 147 88.035 −13.237 0.631 1.00 33.19  258 C LYS A 147 88.933 −14.018 1.577 1.00 33.69  259 O LYS A 147 90.160 −13.941 1.450 1.00 33.61  260 CB LYS A 147 88.113 −11.124 0.937 1.00 35.09  261 CG LYS A 147 87.594 −10.845 −0.194 1.00 37.87  262 CD LYS A 147 88.354 −9.540 −0.293 1.00 39.84  263 CE LYS A 147 88.103 −8.652 0.904 1.00 43.26  264 NZ LYS A 147 88.602 −7.248 0.739 1.00 45.31  265 N THR A 148 88.360 −14.796 2.487 1.00 31.96  266 CA THR A 148 89.108 −15.593 3.444 1.00 30.46  267 C THR A 148 89.841 −16.711 2.711 1.00 32.06  268 O THR A 148 91.043 −16.921 2.873 1.00 30.77  269 CB THR A 148 88.182 −16.136 4.545 1.00 28.74  270 OG1 THR A 148 87.559 −15.026 5.205 1.00 25.09  271 CG2 THR A 148 88.854 −16.928 5.658 1.00 29.31  272 N THR A 149 89.131 −17.425 1.847 1.00 31.51  273 CA THR A 149 89.650 −18.565 1.097 1.00 32.38  274 C THR A 149 90.032 −18.207 −0.336 1.00 34.28  275 O THR A 149 90.843 −18.860 −0.978 1.00 34.35  276 CB THR A 149 88.573 −19.672 1.002 1.00 31.79  277 OG1 THR A 149 87.433 −19.098 0.347 1.00 31.53  278 CG2 THR A 149 88.174 −20.139 2.387 1.00 31.56  279 N GLY A 150 89.415 −17.156 −0.867 1.00 34.16  280 CA GLY A 150 89.621 −16.692 −2.232 1.00 35.07  281 C GLY A 150 88.528 −17.240 −3.148 1.00 34.60  282 O GLY A 150 88.453 −16.846 −4.298 1.00 34.70  283 N GLU A 151 87.706 −18.163 −2.651 1.00 34.79  284 CA GLU A 151 86.647 −18.768 −3.457 1.00 36.01  285 C GLU A 151 85.618 −17.746 −3.946 1.00 35.57  286 O GLU A 151 85.046 −16.957 −3.184 1.00 32.89  287 CB GLU A 151 85.878 −19.866 −2.699 1.00 36.86  288 CG GLU A 151 84.457 −20.388 −2.912 1.00 39.81  289 CD GLU A 151 83.800 −21.357 −1.955 1.00 41.00  290 OE1 GLU A 151 83.941 −21.618 −0.761 1.00 20.00  291 OE2 GLU A 151 82.953 −21.888 −2.659 1.00 20.00  292 N LYS A 152 85.373 −17.792 −5.258 1.00 34.10  293 CA LYS A 152 84.388 −16.920 −5.880 1.00 33.14  294 C LYS A 152 83.100 −17.721 −5.895 1.00 32.88  295 O LYS A 152 83.174 −18.923 −6.156 1.00 34.46  296 CB LYS A 152 84.713 −16.397 −7.291 1.00 33.96  297 CG LYS A 152 86.053 −15.890 −7.831 1.00 20.00  298 CD LYS A 152 86.300 −15.397 −9.258 1.00 20.00  299 CE LYS A 152 87.720 −14.878 −9.009 1.00 20.00  300 NZ LYS A 152 88.820 −14.900 −9.971 1.00 20.00  301 N ILE A 153 81.971 −17.105 −5.571 1.00 30.39  302 CA ILE A 153 80.697 −17.797 −5.515 1.00 30.58  303 C ILE A 153 79.726 −37.261 −6.561 1.00 30.18  304 O ILE A 153 79.369 −16.087 −6.544 1.00 29.54  305 CB ILE A 153 80.079 −17.596 −4.102 1.00 30.99  306 CG1 ILE A 153 81.005 −18.163 −3.015 1.00 32.60  307 CG2 ILE A 183 78.708 −18.243 −4.058 1.00 30.51  308 CD1 ILE A 153 80.665 −17.636 −1.620 1.00 33.71  309 N PRO A 154 79.304 −18.086 −7.516 1.00 30.89  310 CA PRO A 154 78.425 −17.617 −8.577 1.00 29.91  311 C PRO A 154 77.070 −17.092 −8.125 1.00 29.11  312 O PRO A 154 76.389 −17.689 −7.291 1.00 28.76  313 CB PRO A 154 78.239 18.829 −9.471 1.00 30.32  314 CG PRO A 154 79.208 −19.853 −9.041 1.00 31.95  315 CD PRO A 154 79.709 −19.499 −7.665 1.00 30.13  316 N VAL A 155 76.635 −15.979 −8.687 1.00 29.63  317 CA VAL A 155 75.325 −15.376 −8.443 3.00 30.78  318 C VAL A 155 74.378 −15.940 −9.509 1.00 30.85  319 O VAL A 155 74.696 −15.745 −10.690 1.00 30.08  320 CB VAL A 155 75.011 −13.871 −8.530 1.00 30.85  321 CG1 VAL A 155 73.695 −13.215 −8.115 1.00 20.00  322 CG2 VAL A 155 76.117 −13.400 −7.604 1.00 29.33  323 N THR A 156 73.320 −16.648 −9.159 1.00 29.83  324 CA THR A 156 72.450 −17.270 −10.144 3.00 31.67  325 C THR A 156 71.245 −16.427 −10.562 1.00 32.89  326 O THR A 156 70.632 −16.699 −11.621 1.00 32.33  327 CB THR A 156 71.956 −18.634 −9.635 1.00 31.70  328 OG1 THR A 156 71.092 −18.419 −8.515 1.00 31.91  329 CG2 THR A 156 73.150 −19.479 −9.186 1.00 32.24  330 N SER A 157 70.880 −15.436 −9.730 1.00 31.06  331 CA SER A 157 69.833 −14.506 −10.141 1.00 30.56  332 C SER A 157 69.803 −13.227 −9.308 1.00 29.60  333 O SER A 157 70.337 −13.169 −8.195 1.00 27.35  334 CB SER A 157 68.491 −15.222 −10.214 1.00 32.34  335 OG SER A 157 67.810 −15.173 −9.012 1.00 35.08  336 N ALA A 158 69.446 −12.117 −9.959 1.00 26.45  337 CA ALA A 158 69.453 −10.774 −9.423 1.00 27.24  338 C ALA A 158 68.152 −10.053 −9.765 1.00 30.18  339 O ALA A 158 67.765 −9.918 −10.959 1.00 30.53  340 CB ALA A 158 70.645 −10.022 −9.985 1.00 26.36  341 N VAL A 159 67.340 −9.812 −8.734 1.00 28.12  342 CA VAL A 159 66.000 −9.269 −8.930 1.00 28.80  343 C VAL A 159 65.789 −8.029 −8.074 1.00 28.52  344 O VAL A 159 66.627 −7.709 −7.226 1.00 25.60  345 CB VAL A 159 64.846 −10.243 −8.667 1.00 29.04  346 CG1 VAL A 159 64.965 −11.513 −9.494 1.00 29.16  347 CG2 VAL A 159 64.667 −10.636 −7.188 1.00 27.70  348 N SER A 160 64.643 −7.357 −8.283 1.00 28.60  349 CA SER A 160 64.422 −6.159 −7.460 1.00 27.56  350 C SER A 160 63.738 −6.562 −6.141 1.00 27.31  351 O SER A 160 62.904 −7.468 −6.153 1.00 25.37  352 CB SER A 160 63.626 −5.076 −8.149 1.00 28.21  353 OG SER A 160 63.262 −4.072 −7.188 1.00 25.98  354 N ALA A 161 64.205 −5.955 −5.033 1.00 25.91  355 CA ALA A 161 63.629 −6.241 −3.731 1.00 25.68  356 C ALA A 161 62.547 −5.238 −3.329 1.00 26.62  357 O ALA A 161 61.886 −5.395 −2.296 1.00 23.95  358 CB ALA A 161 64.715 −6.344 −2.642 1.00 25.65  359 N ASN A 162 62.257 −4.216 −4.131 1.00 26.84  360 CA ASN A 162 61.183 −3.278 −3.763 1.00 27.62  361 C ASN A 162 59.841 −3.987 −3.818 1.00 28.07  362 O ASN A 162 59.547 −4.755 −4.741 1.00 28.17  363 CB ASN A 162 61.196 −2.092 −4.718 1.00 28.34  364 CG ASN A 162 62.395 −1.174 −4.643 1.00 29.74  365 OD1 ASN A 162 62.886 −0.911 −3.535 1.00 30.40  366 ND2 ASN A 162 62.829 −0.625 −5.774 1.00 27.62  367 N PRO A 163 58.979 −3.767 −2.828 1.00 27.79  368 CA PRO A 163 57.661 −4.372 −2.786 1.00 26.20  369 C PRO A 163 56.742 −3.804 −3.860 1.00 25.38  370 O PRO A 163 56.967 −2.735 −4.449 1.00 24.29  371 CB PRO A 163 57.181 −4.066 −1.369 1.00 27.88  372 CG PRO A 163 57.870 −2.776 −1.027 1.00 28.89  373 CD PRO A 163 59.234 −2.875 −1.661 1.00 27.81  374 N VAL A 164 55.717 −4.569 −4.208 1.00 25.30  375 CA VAL A 164 54.721 −4.187 −5.220 1.00 25.51  376 C VAL A 164 53.339 −4.283 −4.585 1.00 24.80  377 O VAL A 164 52.995 −5.340 −4.040 1.00 26.11  378 CB VAL A 164 54.802 −5.048 −6.493 1.00 24.71  379 CG1 VAL A 164 53.663 −4.752 −7.467 1.00 26.19  380 CG2 VAL A 164 56.125 −4.811 −7.253 1.00 25.42  381 N THR A 165 52.538 −3.233 −4.606 1.00 24.33  382 CA THR A 165 51.200 −3.270 −4.032 1.00 25.19  383 C THR A 165 58.176 −3.008 −5.166 1.00 24.41  384 O THR A 165 49.956 −1.847 −5.503 1.00 21.40  385 CB THR A 165 50.966 −2.262 −2.897 1.00 26.83  386 OG1 THR A 165 51.832 −2.523 −1.774 1.00 28.11  387 CG2 THR A 165 49.533 −2.347 −2.377 1.00 25.74  388 N ALA A 166 49.546 −4.081 −5.643 1.00 22.25  389 CA ALA A 166 48.656 −3.909 −6.820 1.00 23.36  390 C ALA A 166 47.323 −4.512 −8.453 1.00 22.56  391 O ALA A 166 47.351 −5.703 −6.108 1.00 24.73  392 CB ALA A 166 49.294 −4.589 −8.031 1.00 19.57  393 N VAL A 167 46.229 −3.768 −6.464 1.00 22.47  394 CA VAL A 167 44.939 −4.309 −6.043 1.00 19.46  395 C VAL A 167 43.980 −4.333 −7.248 1.00 21.03  396 O VAL A 167 43.901 −3.309 −7.917 1.00 18.72  397 CB VAL A 167 44.310 −3.476 −4.911 1.00 20.70  398 CG1 VAL A 167 42.832 −3.503 −4.525 1.00 18.70  399 CG2 VAL A 167 45.155 −3.486 −3.651 1.00 22.11  400 N LEU A 168 43.264 −5.454 −7.447 1.00 19.41  401 CA LEU A 168 42.257 −5.482 −8.519 1.00 18.94  402 C LEU A 168 41.053 −4.647 −8.099 1.00 20.89  403 O LEU A 168 40.431 −4.955 −7.048 1.00 21.09  404 CB LEU A 168 41.808 −6.925 −8.770 1.00 18.27  405 CG LEU A 168 40.646 −7.136 −9.739 1.00 18.57  406 CD1 LEU A 168 41.115 −6.720 −11.135 1.00 17.67  407 CD2 LEU A 168 40.166 −8.607 −9.767 1.00 17.71  408 N VAL A 169 40.726 −3.598 −8.865 1.00 20.18  409 CA VAL A 169 39.571 −2.758 −8.519 1.00 19.68  410 C VAL A 169 38.501 −2.816 −9.592 1.00 20.02  411 O VAL A 169 38.871 −2.925 −10.765 1.00 19.91  412 CB VAL A 169 39.943 −1.260 −8.324 1.00 19.72  413 CG1 VAL A 169 40.903 −1.142 −7.131 1.00 17.22  414 CG2 VAL A 169 40.600 −0.612 −9.541 1.00 18.93  415 N GLY A 178 37.224 −2.742 −9.246 1.00 18.55  416 CA GLY A 170 36.172 −2.790 −10.248 1.00 18.73  417 C GLY A 170 34.791 −3.031 −9.664 1.00 17.66  418 O GLY A 170 34.639 −3.096 −8.438 1.00 17.25  419 N ASP A 171 33.806 −3.317 −10.580 1.00 18.35  420 CA ASP A 171 32.470 −3.653 −10.006 1.00 22.28  421 C ASP A 171 32.356 −5.172 −9.771 1.00 22.87  422 O ASP A 171 31.275 −5.671 −9.490 1.00 21.75  423 CB ASP A 171 31.304 −3.164 −10.866 1.00 22.13  424 CG ASP A 171 31.364 −3.728 −12.276 1.00 24.79  425 OD1 ASP A 171 32.272 −4.532 −12.592 1.00 24.08  426 OD2 ASP A 171 30.463 −3.373 −13.068 1.00 25.44  427 N LEU A 172 33.459 −5.907 −9.824 1.00 23.38  428 CA LEU A 172 33.556 −7.317 −9.519 1.00 23.45  429 C LEU A 172 34.101 −7.426 −8.093 1.00 23.46  430 O LEU A 172 34.338 −8.531 −7.601 1.00 23.89  431 CB LEU A 172 34.488 −8.066 −10.492 1.00 23.96  432 CG LEU A 172 35.716 −7.388 −11.089 1.00 23.60  433 CD1 LEU A 172 36.700 −6.874 −10.024 1.00 23.92  434 CD2 LEU A 172 36.501 −8.286 −12.049 1.00 22.64  435 N GLN A 173 34.427 −6.304 −7.425 1.00 22.02  436 CA GLN A 173 35.116 −6.409 −6.144 1.00 23.00  437 C GLN A 173 34.301 −7.061 −5.012 1.00 25.30  438 O GLN A 173 34.956 −7.778 −4.222 1.00 23.45  439 CB GLN A 173 35.715 −5.085 −5.640 1.00 19.82  440 CG GLN A 173 37.222 −5.133 −5.502 1.00 20.64  441 CD GLN A 173 37.865 −3.790 −5.190 1.00 20.89  442 OE1 GLN A 173 38.776 −3.712 −4.337 1.00 21.68  443 NE2 GLN A 173 37.472 −2.762 −5.917 1.00 14.10  444 N GLN A 174 33.011 −6.766 −4.897 1.00 27.15  445 CA GLN A 174 32.211 −7.350 −3.808 1.00 30.17  446 C GLN A 174 32.010 −8.853 −3.980 1.00 29.95  447 O GLN A 174 32.162 −9.17 −3.030 1.00 29.74  448 CB GLN A 174 30.806 −6.738 −3.686 1.00 30.31  449 CG GLN A 174 30.791 −5.300 −3.184 1.00 31.02  450 CD GLN A 174 29.381 −4.727 −3.153 1.00 32.11  451 OE1 GLN A 174 28.641 −4.750 −4.123 1.00 32.20  452 NE2 GLN A 174 29.058 −4.103 −2.011 1.00 32.45  453 N ALA A 175 31.859 −9.290 −5.225 1.00 30.17  454 CA ALA A 175 31.793 −10.722 −5.537 1.00 30.64  455 C ALA 175 33.072 −11.450 −5.174 1.00 30.81  456 O ALA A 175 33.044 −12.667 −4.926 1.00 31.59  457 CB ALA A 175 31.469 −10.864 −7.023 1.00 30.89  458 N LEU A 176 34.188 −10.738 −5.050 1.00 29.83  459 CA LEU A 176 35.474 −11.299 −4.683 1.00 30.69  460 C LEU A 176 35.799 −11.058 −3.218 1.00 31.12  461 O LEU A 176 36.912 −11.315 −2.771 1.00 31.07  462 CB LEU A 176 36.587 −10.806 −5.622 1.00 30.20  463 CG LEU A 176 36.490 −11.210 −7.098 1.00 30.54  464 CD1 LEU A 176 37.534 −10.515 −7.971 1.00 28.99  465 CD2 LEU A 176 36.726 −12.713 −7.263 1.00 30.40  466 N GLY A 177 34.829 −10.590 −2.432 1.00 33.38  467 CA GLY A 177 34.977 −10.426 −1.004 1.00 34.48  468 C GLY A 177 35.277 −9.040 −0.468 1.00 36.08  469 O GLY A 177 35.331 −8.865 0.764 1.00 35.24  470 N ALA A 178 35.543 −8.079 −1.354 1.00 34.40  471 CA ALA A 178 35.818 −6.733 −0.871 1.00 34.80  472 C ALA A 178 34.509 −6.155 −0.321 1.00 33.76  473 O ALA A 178 33.439 −6.440 −0.842 1.00 33.43  474 CB ALA A 178 36.359 −5.829 −1.970 1.00 32.96  475 N ALA A 179 34.601 −5.282 0.670 1.00 33.57  476 CA ALA A 179 33.434 −4.614 1.223 1.00 32.22  477 C ALA 179 32.707 −3.731 0.213 1.00 30.62  478 O ALA A 179 31.466 −3.697 0.192 1.00 30.86  479 CB ALA A 179 33.856 −3.733 2.401 1.00 34.25  480 N ASN A 180 33.420 −2.907 −0.561 1.00 29.04  481 CA ASN A 180 32.851 −2.015 −1.558 1.00 28.58  482 C ASN A 180 33.499 −2.211 −2.939 1.00 27.39  483 O ASN A 180 34.638 −2.689 −3.042 1.00 26.95  484 CB ASN A 180 32.957 −0.521 −1.148 1.00 29.90  485 CG ASN A 180 32.103 −0.258 0.104 1.00 31.68  486 OD1 ASN A 180 30.885 −0.552 0.100 1.00 34.34  487 ND2 ASN A 180 32.750 0.063 1.209 1.00 32.41  488 N ASN A 181 32.825 −1.832 −4.017 1.00 25.75  489 CA ASN A 181 33.370 −1.875 −5.372 1.00 25.22  490 C ASN A 181 34.287 −0.683 −5.625 1.00 24.74  491 O ASN A 181 34.253 0.299 −4.849 1.00 23.10  492 CB ASN A 181 32.221 −1.881 6.393 1.00 24.36  493 CG ASN A 181 31.526 −3.216 −6.503 1.00 23.81  494 OD1 ASN A 181 30.312 −3.231 −6.776 1.00 25.93  495 ND2 ASN A 181 32.208 −4.326 −6.339 1.00 19.94  496 N TRP A 182 35.132 −0.743 −6.657 1.00 23.37  497 CA TRP A 182 36.096 0.317 −6.986 1.00 22.89  498 C TRP A 182 36.812 0.884 −5.748 1.00 24.90  499 O TRP A 182 36.686 2.061 −5.356 1.00 22.19  500 CB TRP A 182 35.440 1.390 −7.842 1.00 21.88  501 CG TRP A 182 34.968 0.888 −9.213 1.00 21.19  502 CD1 TRP A 182 33.661 0.662 −9.556 1.00 20.22  503 CD2 TRP A 182 35.772 0.587 −10.354 1.00 20.33  504 NE1 TRP A 182 33.620 0.238 −10.890 1.00 21.14  505 CE2 TRP A 182 34.899 0.206 −11.396 1.00 20.92  506 CE3 TRP A 182 37.140 0.646 −10.652 1.00 19.83  507 CZ2 TRP A 182 35.335 −0.126 −12.679 1.00 19.37  508 CZ3 TRP A 182 37.588 0.290 −11.911 1.00 20.08  509 CH2 TRP A 182 36.682 −0.111 −12.925 1.00 18.62  510 N SER A 183 37.553 −0.028 −5.091 1.00 24.20  511 CA SER A 183 38.166 0.298 −3.787 1.00 25.99  512 C SER A 183 39.619 −0.056 −3.755 1.00 25.00  513 O SER A 183 40.038 −1.222 −3.552 1.00 24.72  514 CB SER A 183 37.250 −0.396 −2.744 1.00 27.68  515 OG SER A 183 37.806 −0.303 −1.422 1.00 31.94  516 N PRO A 184 40.504 0.901 −3.999 1.00 24.27  517 CA PRO A 184 41.936 0.660 −4.076 1.00 25.54  518 C PRO A 184 42.583 0.218 −2.771 1.00 27.83  519 O PRO A 184 43.702 −0.312 −2.819 1.00 26.74  520 CB PRO A 184 42.567 2.002 −4.480 1.00 25.19  521 CG PRO A 184 41.436 2.850 −4.939 1.00 27.00  522 CD PRO A 184 40.171 2.317 −4.293 1.00 25.48  523 N ASP A 185 41.953 0.501 −1.660 1.00 28.67  524 CA ASP A 185 42.469 0.243 −0.330 1.00 35.01  525 C ASP A 185 42.168 −1.154 0.186 1.00 32.77  526 O ASP A 185 42.631 −1.481 1.276 1.00 32.78  527 CB ASP A 185 41.794 1.331 0.575 1.00 40.22  528 CG ASP A 185 40.328 0.971 0.823 1.00 45.75  529 OD1 ASP A 185 39.796 −0.145 0.631 1.00 49.67  530 OD2 ASP A 185 39.665 1.968 1.250 1.00 48.92  531 N ASP A 186 41.216 −1.836 −0.471 1.00 30.11  532 CA ASP A 186 40.727 3.109 0.072 1.00 29.50  533 C ASP A 186 41.595 −4.279 −0.355 1.00 28.84  534 O ASP A 186 41.578 −4.767 −1.473 1.00 26.82  535 CB ASP A 186 39.253 −3.271 −0.280 1.00 29.89  536 CG ASP A 186 38.521 −4.309 0.548 1.00 30.33  537 OD1 ASP A 186 39.135 −5.357 0.847 1.00 30.32  538 OD2 ASP A 186 37.337 −4.120 0.897 1.00 29.44  539 N ASP A 187 42.390 −4.757 0.617 1.00 28.04  540 CA ASP A 187 43.314 −5.849 0.376 1.00 28.05  541 C ASP A 187 42.680 −7.218 0.204 1.00 26.64  542 O ASP A 187 43.469 −8.146 0.051 1.00 26.92  543 CB ASP A 187 44.447 −5.977 1.403 1.00 29.12  544 CG ASP A 187 45.562 −5.006 1.075 1.00 29.66  545 OD1 ASP A 187 45.560 −4.414 −0.035 1.00 29.31  546 OD2 ASP A 187 46.419 −4.719 1.940 1.00 30.32  547 N HIS A 188 41.382 −7.380 0.101 1.00 25.81  548 CA HIS A 188 40.750 −8.635 −0.234 1.00 28.57  549 C HIS A 188 41.034 −8.980 −1.719 1.00 28.04  550 O HIS A 188 40.988 −10.162 −2.051 1.00 25.11  551 CB HIS A 188 39.247 −8.622 0.001 1.00 31.30  552 CG HIS A 188 38.773 −8.598 1.420 1.00 35.25  553 ND1 HIS A 188 38.178 −9.695 2.019 1.00 36.56  554 CD2 HIS A 188 38.785 −7.621 2.366 1.00 36.05  555 CE1 HIS A 188 37.843 −9.392 3.263 1.00 37.12  556 NE2 HIS A 188 38.209 −8.137 3.496 1.00 38.08  557 N THR A 189 41.419 −8.003 −2.549 1.00 25.78  558 CA THR A 189 41.749 −8.277 −3.944 1.00 25.63  559 C THR A 189 43.164 −7.831 −4.295 1.00 26.53  560 O THR A 189 43.525 −7.508 −5.446 1.00 25.53  561 CB THR A 189 40.736 −7.696 −4.945 1.00 24.83  562 OG1 THR A 189 40.551 −6.312 −4.648 1.00 23.22  563 CG2 THR A 189 39.397 −8.428 −4.913 1.00 24.10  564 N LEU A 190 44.036 −7.871 −3.278 1.00 24.47  565 CA LEU A 190 45.446 −7.592 −3.497 1.00 25.02  566 C LEU A 190 46.106 −8.740 −4.276 1.00 25.66  567 O LEU A 190 45.947 −9.871 −3.821 1.00 24.54  568 CB LEU A 190 46.115 −7.493 −2.126 1.00 25.49  569 CG LEU A 190 47.612 −7.221 −2.066 1.00 26.63  570 CD1 LEU A 190 47.961 −5.811 −2.561 1.00 26.87  571 CD2 LEU A 190 48.107 −7.483 −0.649 1.00 26.92  572 N LEU A 191 46.785 −8.501 −5.397 1.00 23.25  573 CA LEU A 191 47.424 −9.589 −6.120 1.00 22.73  574 C LEU A 191 48.627 −10.118 −5.353 1.00 23.44  575 O LEU A 191 49.390 −9.351 −4.748 1.00 21.57  576 CB LEU A 191 47.921 −9.125 −7.510 1.00 21.62  577 CG LEU A 191 46.880 −8.960 −8.614 1.00 21.93  578 CD1 LEU A 191 45.698 −8.077 −8.268 1.00 18.64  579 CD2 LEU A 191 47.599 −8.457 −9.886 1.00 21.63  580 N LYS A 192 48.898 −11.403 −5.497 1.00 23.59  581 CA LYS A 192 50.006 −12.052 −4.827 1.00 24.86  582 C LYS A 192 51.232 −12.227 −5.700 1.00 26.50  583 O LYS A 192 51.100 −12.428 −6.912 1.00 26.86  584 CB LYS A 192 49.560 −13.491 −4.421 1.00 25.31  585 CG LYS A 192 48.449 −13.455 −3.375 1.00 27.13  586 CD LYS A 192 47.815 −14.750 −3.079 0.00 20.00  587 CE LYS A 192 46.420 −14.700 −2.448 0.00 20.00  588 NZ LYS A 192 46.039 −16.034 −1.988 0.00 20.00  589 N LYS A 193 52.413 −12.326 −5.098 1.00 27.68  590 CA LYS A 193 53.593 −12.532 −5.943 1.00 32.22  591 C LYS A 193 53.825 −13.987 −6.288 1.00 32.50  592 O LYS A 193 53.939 −14.822 −5.409 1.00 30.76  593 CB LYS A 193 54.734 −11.805 −5.260 1.00 35.25  594 CG LYS A 193 56.021 −12.513 −4.979 1.00 39.64  595 CD LYS A 193 57.217 −11.595 −5.033 1.00 41.28  596 CE LYS A 193 58.106 −11.653 −3.808 1.00 44.51  597 NZ LYS A 193 59.154 −10.583 −3.791 1.00 45.93  598 N ILE A 194 53.836 −14.305 −7.593 1.00 30.97  599 CA ILE A 194 54.161 −15.631 −8.117 1.00 29.28  600 C ILE A 194 55.654 −15.716 −8.412 1.00 28.94  601 O ILE A 194 56.334 −16.725 −8.177 1.00 28.26  602 CB ILE A 194 53.341 −15.917 −9.394 1.00 30.80  603 CG1 ILE A 194 51.872 −15.560 −9.172 1.00 29.46  604 CG2 ILE A 194 53.505 −17.363 −9.869 1.00 30.31  605 CD1 ILE A 194 51.129 −16.279 −8.076 1.00 29.66  606 N ASN A 195 56.246 −14.658 −8.969 1.00 26.41  607 CA ASN A 195 57.689 −14.582 −9.209 1.00 25.15  608 C ASN A 195 57.982 −13.108 −9.056 1.00 25.32  609 O ASN A 195 57.060 −12.285 −9.010 1.00 24.84  610 CB ASN A 195 58.205 −15.255 −10.468 1.00 26.01  611 CG ASN A 195 58.002 −14.588 −11.816 1.00 23.49  612 OD1 ASN A 195 58.324 −13.419 −11.979 1.00 22.62  613 ND2 ASN A 195 57.463 −15.271 −12.821 1.00 21.61  614 N PRO A 196 59.222 −12.681 −8.921 1.00 27.18  615 CA PRO A 196 59.566 −11.282 −8.695 1.00 27.81  616 C PRO A 196 59.014 −10.304 −9.712 1.00 28.82  617 O PRO A 196 58.874 −9.118 −9.403 1.00 29.64  618 CB PRO A 196 61.088 −11.245 −8.660 1.00 27.55  619 CG PRO A 196 61.562 −12.641 −8.735 1.00 27.99  620 CD PRO A 196 60.400 −13.571 −8.910 1.00 27.24  621 N ASN A 197 58.728 −10.737 −10.939 1.00 28.40  622 CA ASN A 197 58.152 −9.868 −11.964 1.00 27.61  623 C ASN A 197 56.808 −10.412 −12.426 1.00 26.54  624 O ASN A 197 56.446 −10.216 −13.588 1.00 24.74  625 CB ASN A 197 59.156 −9.685 −13.114 1.00 25.82  626 CG ASN A 197 58.874 −8.553 −14.073 1.00 24.90  627 OD1 ASN A 197 58.401 −7.487 −13.679 1.00 25.87  628 ND2 ASN A 197 59.143 −8.694 −15.374 1.00 22.51  629 N LEU A 198 56.003 −11.008 −11.527 1.00 25.03  630 CA LEU A 198 54.709 −11.567 −11.921 1.00 25.50  631 C LEU A 198 53.734 −11.604 −10.757 1.00 24.75  632 O LEU A 198 54.037 −12.353 −9.805 1.00 24.83  633 CB LEU A 198 54.639 −12.947 −12.600 1.00 26.19  634 CG LEU A 198 53.385 −13.711 −13.032 1.00 29.17  635 CD1 LEU A 198 52.653 −13.174 −14.263 1.00 28.46  636 CD2 LEU A 198 54.064 −15.009 −13.469 1.00 31.33  637 N TYR A 199 52.635 −10.883 −10.781 1.00 22.56  638 CA TYR A 199 51.640 −10.794 −9.724 1.00 22.64  639 C TYR A 199 50.281 −11.275 −10.192 1.00 23.37  640 O TYR A.399 49.898 −10.900 −11.326 1.00 21.85  641 CB TYR A 199 51.488 −9.332 −9.172 1.00 22.41  642 CG TYR A 199 52.673 −9.037 −8.251 1.00 24.19  643 CD1 TYR A 199 52.525 −9.019 −6.870 1.00 24.33  644 CD2 TYR A 199 53.955 −8.856 −8.753 1.00 24.63  645 CE1 TYR A 199 53.599 −8.782 −6.021 1.00 23.22  646 CE2 TYR A 199 55.047 −8.650 −7.934 1.00 24.30  647 CZ TYR A 199 54.848 −8.607 −6.552 1.00 25.35  648 OH TYR A 199 55.967 −8.424 −5.758 1.00 25.36  649 N GLN A 200 49.593 −12.153 −9.437 1.00 21.46  650 CA GLN A 200 48.319 −12.703 −9.851 1.00 22.78  651 C GLN A 200 47.308 −12.901 −8.709 1.00 23.92  652 O GLN A 200 47.642 −12.965 −7.529 1.00 23.20  653 CB GLN A 200 48.460 −14.071 −10.554 1.00 23.72  654 CG GLN A 200 49.326 −14.123 −11.818 1.00 23.30  655 CD GLN A 200 49.357 −15.468 −12.509 1.00 24.08  656 OE1 GLN A 200 48.907 −15.563 −13.665 1.00 25.79  657 NE2 GLN A 200 49.802 −1.529 −11.838 1.00 21.68  658 N LEU A 201 46.029 −12.854 −9.068 1.00 22.79  659 CA LEU A 201 44.878 −13.063 −8.223 1.00 23.86  660 C LEU A 201 43.871 −13.926 −8.993 1.00 22.76  661 O LEU A 201 43.615 −13.595 −10.149 1.00 20.39  662 CB LEU A 201 44.180 −11.770 −7.798 1.00 24.31  663 CG LEU A 201 42.984 −11.871 −6.855 1.00 27.82  664 CD1 LEU A 201 43.423 −12.292 −5.451 1.00 28.00  665 CD2 LEU A 201 42.247 −10.531 −6.725 1.00 26.81  666 N SER A 202 43.269 −14.938 −8.367 1.00 21.06  667 CA SER A 202 42.217 15.727 −8.956 1.00 20.94  668 C SER A 202 40.969 −15.724 −8.085 1.00 24.18  669 O SER A 202 41.140 −15.747 −6.843 1.00 26.01  670 CB SER A 202 42.700 −17.198 −9.057 1.00 21.57  671 OG SER A 202 43.669 −17.342 −10.101 1.00 24.54  672 N GLY A 203 39.768 −15.823 −8.623 1.00 24.80  673 CA GLY A 203 38.565 −15.892 −7.834 1.00 25.89  674 C GLY A 203 37.359 −16.159 −8.711 1.00 28.12  675 O GLY A 203 37.385 −15.914 −9.919 1.00 28.11  676 N THR A 204 36.305 −16.716 −8.088 1.00 27.74  677 CA THR A 204 35.097 −17.110 −8.779 1.00 26.86  678 C THR A 204 34.105 −15.971 −8.927 1.00 26.50  679 O THR A 204 33.813 −15.312 −7.936 1.00 26.91  680 CB THR A 204 34.383 −18.207 −7.933 1.00 29.21  681 OG1 THR A 204 35.262 −19.322 −7.816 1.00 28.46  682 CG2 THR A 204 33.059 −18.617 −8.581 1.00 28.38  683 N LEU A 205 33.575 −15.738 −10.119 1.00 25.28  684 CA LEU A 205 32.594 −14.705 −10.324 1.00 27.14  685 C LEU A 205 31.303 −15.289 −10.898 1.00 29.05  686 O LEU A 205 31.325 −16.121 −11.802 1.00 27.54  687 CB LEU A 205 33.139 −13.666 −11.307 1.00 27.39  688 CG LEU A 205 34.340 −12.803 −10.896 1.00 27.95  689 CD1 LEU A 205 34.858 −12.022 −12.101 1.00 27.28  690 CD2 LEU A 205 33.999 −11.861 −9.743 1.00 29.19  691 N PRO A 206 30.154 −14.795 −10.441 1.00 30.40  692 CA PRO A 206 28.870 −15.199 −11.005 1.00 30.93  693 C PRO A 206 28.882 −14.794 −12.473 1.00 31.99  694 O PRO A 206 29.702 −13.916 −12.809 1.00 32.25  695 CB PRO A 206 27.830 −14.370 −10.241 1.00 30.06  696 CG PRO A 206 28.518 −13.896 −9.020 1.00 30.95  697 CD PRO A 206 30.006 −13.818 −9.345 1.00 31.23  698 N ALA A 207 27.959 −15.236 −13.292 1.00 30.94  699 CA ALA A 207 27.829 −14.752 −14.647 1.00 32.79  700 C ALA A 207 27.525 −13.250 −14.646 1.00 33.93  701 O ALA A 207 26.875 −12.784 −13.698 1.00 33.84  702 CB ALA A 207 26.644 −15.405 −15.344 1.00 33.37  703 N GLY A 208 27.891 −12.554 −15.717 1.00 33.30  704 CA GLY A 208 27.627 −11.117 −15.815 1.00 33.40  705 C GLY A 208 28.764 −10.431 −16.590 1.00 34.81  706 O GLY A 208 29.748 −11.089 −16.954 1.00 34.75  707 N THR A 209 28.631 −9.147 −16.855 1.00 33.68  708 CA THR A 209 29.649 −8.364 −17.553 1.00 35.01  709 C THR A 209 30.168 −7.337 −16.549 1.00 32.85  710 O THR A 209 29.371 −6.687 −15.843 1.00 31.81  711 CB THR A 209 29.126 −7.714 −18.837 1.00 37.54  712 OG1 THR A 209 30.036 −6.711 −19.353 1.00 40.79  713 CG2 THR A 209 27.808 −7.044 −18.521 1.00 38.82  714 N TYR A 210 31.475 −7.356 −16.327 1.00 28.47  715 CA TYR A 210 32.119 −6.499 −15.331 1.00 25.61  716 C TYR A 210 33.148 −5.574 −15.968 1.00 23.20  717 O TYR A 210 33.511 −5.730 −17.129 1.00 20.43  718 CB TYR A 210 32.853 −7.361 −14.285 1.00 25.13  719 CG TYR A 210 32.043 −8.437 −13.604 1.00 25.77  720 CD1 TYR A 210 31.418 −8.187 −12.385 1.00 26.19  721 CD2 TYR A 210 31.878 −9.699 −14.159 1.00 26.65  722 CE1 TYR A 210 30.647 −9.141 −11.755 1.00 25.94  723 CE2 TYR A 210 31.129 −10.686 −13.531 1.00 26.59  724 CZ TYR A 210 30.508 −10.392 −12.330 1.00 27.30  725 OH TYR A 210 29.776 −11.352 −11.675 1.00 28.27  726 N GLN A 211 33.707 −4.664 −15.180 1.00 21.51  727 CA GLN A 211 34.770 −3.769 −15.611 1.00 21.91  728 C GLN A 211 35.851 −3.700 −14.517 1.00 20.11  729 O GLN A 211 35.444 −3.737 −13.367 1.00 19.22  730 CB GLN A 211 34.270 −2.358 −15.949 1.00 20.26  731 CG GLN A 211 33.515 −2.252 −17.274 1.00 21.03  732 CD GLN A 211 32.948 −0.889 −17.595 1.00 21.84  733 OE1 GLN A 211 32.192 −0.698 −18.590 1.00 23.95  734 NE2 GLN A 211 33.387 0.136 −16.876 1.00 20.75  735 N TYR A 212 37.144 −3.613 −14.861 1.00 18.80  736 CA TYR A 212 38.126 −3.616 −13.782 1.00 19.43  737 C TYR A 212 39.418 −2.932 −14.206 1.00 20.03  738 O TYR A 212 39.722 −2.780 −15.384 1.00 17.17  739 CB TYR A 212 38.434 −5.067 −13.433 1.00 20.14  740 CG TYR A 212 39.327 −5.644 −14.475 1.00 20.47  741 CD1 TYR A 212 38.790 −6.478 −15.451 1.00 19.52  742 CD2 TYR A 212 40.715 −5.503 −14.382 1.00 19.82  743 CE1 TYR A 212 39.622 −7.192 −16.297 1.00 18.82  744 CE2 TYR A 212 41.549 −6.216 −15.233 1.00 20.89  745 CZ TYR A 212 41.006 −7.061 −16.184 1.00 19.83  746 OH TYR A 212 41.824 −7.773 −17.038 1.00 20.51  747 N LYS A 213 40.166 −2.472 −13.189 1.00 18.54  748 CA LYS A 213 41.504 −1.960 −13.442 1.00 19.62  749 C LYS A 213 42.481 −2.457 −12.374 1.00 19.10  750 O LYS A 213 42.131 −3.179 −11.451 1.00 21.19  751 CB LYS A 213 41.449 −0.429 −13.444 1.00 20.40  752 CG LYS A 213 40.902 0.131 −14.757 1.00 19.33  753 CD LYS A 213 41.325 1.584 −14.995 1.00 21.89  754 CE LYS A 213 40.838 2.532 −13.895 1.00 24.44  755 NZ LYS A 213 41.231 3.905 −14.220 1.00 26.58  756 N ILE A 214 43.762 −2.212 −12.362 1.00 18.54  757 CA ILE A 214 44.727 −2.502 −11.342 1.00 19.13  758 C ILE A 214 45.225 −1.142 −10.779 1.00 20.65  759 O ILE A 214 45.930 −0.422 −11.489 1.00 17.06  760 CB ILE A 214 45.969 −3.255 −11.847 1.00 19.87  761 CG1 ILE A 214 45.679 −4.554 −12.610 1.00 20.30  762 CG2 ILE A 214 46.957 −3.514 −10.703 1.00 18.99  763 CD1 ILE A 214 44.772 −5.587 −11.986 1.00 19.54  764 N ALA A 215 44.970 −0.894 −9.489 1.00 21.29  765 CA ALA A 215 45.406 0.360 −8.837 1.00 21.91  766 C ALA A 215 46.590 0.082 −7.923 1.00 22.37  767 O ALA A 215 46.588 −0.953 −7.226 1.00 21.58  768 CB ALA A 215 44.222 0.911 −7.989 1.00 20.97  769 N LEU A 216 47.641 0.873 −7.988 1.00 21.99  770 CA LEU A 216 48.845 0.752 −7.159 1.00 22.55  771 C LEU A 216 48.759 1.510 −5.817 1.00 24.71  772 O LEU A 216 48.006 2.458 −5.641 1.00 22.08  773 CB LEU A 216 50.029 1.290 −7.964 1.00 23.76  774 CG LEU A 216 50.319 0.462 −9.216 1.00 22.14  775 CD1 LEU A 216 51.686 0.786 −9.825 1.00 22.16  776 CD2 LEU A 216 50.316 −1.042 −8.946 1.00 24.20  777 N ASP A 217 49.548 1.000 −4.839 1.00 24.74  778 CA ASP A 217 49.861 1.748 −3.610 1.00 28.00  779 C ASP A 217 48.639 2.264 −2.839 1.00 29.70  780 O ASP A 217 48.678 3.296 −2.182 1.00 30.51  781 CB ASP A 217 50.783 2.907 −3.980 1.00 27.70  782 CG ASP A 217 52.039 2.351 −4.632 1.00 28.23  783 OD1 ASP A 217 52.497 1.300 −4.187 1.00 25.51  784 OD2 ASP A 217 52.537 2.962 −5.574 1.00 29.46  785 N HIS A 218 47.515 1.528 −2.878 1.00 28.93  786 CA HIS A 218 46.336 1.913 −2.179 1.00 31.04  787 C HIS A 218 45.820 3.308 −2.512 1.00 32.01  788 O HIS A 218 45.314 3.968 −1.594 1.00 33.76  789 CB HIS A 218 46.580 1.848 −0.656 1.00 32.62  790 CG HIS A 218 46.763 0.494 −0.095 1.00 34.70  791 ND1 HIS A 218 46.289 −0.669 −0.712 1.00 35.05  792 CD2 HIS A 218 47.351 0.031 1.035 1.00 36.61  793 CE1 HIS A 218 46.572 −1.745 −0.006 1.00 35.70  794 NE2 HIS A 218 47.230 −1.346 1.068 1.00 38.00  795 N SER A 219 45.873 3.742 −3.746 1.00 30.50  796 CA SER A 219 45.437 5.088 −4.114 1.00 29.81  797 C SER A 219 44.927 5.097 −5.553 1.00 28.38  798 O SER A 219 45.236 4.171 −6.317 1.00 26.48  799 CB SER A 219 46.673 5.978 −3.940 1.00 31.74  800 OG SER A 219 46.686 7.146 −4.725 1.00 33.53  801 N TRP A 220 44.295 6.201 −5.943 1.00 26.47  802 CA TRP A 220 43.880 6.481 −7.293 1.00 27.86  803 C TRP A 220 44.969 7.170 −8.118 1.00 28.10  804 O TRP A 220 44.749 7.371 −9.326 1.00 27.08  805 CB TRP A 220 42.620 7.353 −7.351 1.00 28.03  806 CG TRP A 220 41.346 6.631 −7.044 1.00 27.68  807 CD1 TRP A 220 40.441 6.925 −6.071 1.00 26.78  808 CD2 TRP A 220 40.843 5.467 −7.730 1.00 26.84  809 NE1 TRP A 220 39.395 6.022 −6.110 1.00 27.04  810 CE2 TRP A 220 39.632 5.109 −7.121 1.00 26.56  811 CE3 TRP A 220 41.320 4.690 −8.788 1.00 27.09  812 CZ2 TRP A 220 38.876 4.018 −7.520 1.00 25.18  813 CZ3 TRP A 220 40.583 3.615 −9.210 1.00 26.81  814 CH2 TRP A 220 39.369 3.287 −8.557 1.00 26.52  815 N ASN A 221 46.109 7.509 −7.535 1.00 27.91  816 CA ASN A 221 47.167 8.184 −8.277 1.00 29.33  817 C ASN A 221 47.613 7.441 −9.528 1.00 29.98  818 O ASN A 221 47.834 8.056 −10.580 1.00 29.96  819 CB ASN A 221 48.384 8.377 −7.354 1.00 32.21  820 CG ASN A 221 48.207 9.429 −6.270 1.00 35.96  821 OD1 ASN A 221 47.216 10.178 −6.276 1.00 39.36  822 ND2 ASN A 221 49.141 9.546 −5.324 1.00 35.91  823 N THR A 222 47.864 6.135 −9.421 1.00 28.62  824 CA THR A 222 48.373 5.326 −10.511 1.00 27.05  825 C THR A 222 47.570 4.034 −10.661 1.00 25.67  826 O THR A 222 47.542 3.226 −9.734 1.00 22.27  827 CB THR A 222 49.869 5.008 −10.320 1.00 28.65  828 OG1 THR A 222 50.605 6.252 −10.393 1.00 30.47  829 CG2 THR A 222 50.488 4.129 −11.433 1.00 28.53  830 N SER A 223 47.016 3.848 −11.867 1.00 23.93  831 CA SER A 223 46.277 2.629 −12.399 1.00 22.41  832 C SER A 223 46.504 2.179 −13.656 1.00 22.11  833 O SER A 223 46.870 3.009 −14.521 1.00 20.63  834 CB SER A 223 44.791 2.770 −11.925 1.00 21.37  835 OG SER A 223 44.098 3.680 −12.748 1.00 21.13  836 N TYR A 224 46.306 0.904 −13.924 1.00 19.54  837 CA TYR A 224 46.392 0.447 −35.308 1.00 20.33  838 C TYR A 224 45.256 −0.515 −15.656 1.00 23.40  839 O TYR A 224 44.678 −1.178 −14.806 1.00 21.40  840 CB TYR A 224 47.730 −0.269 −15.496 1.00 20.56  841 CG TYR A 224 48.851 0.617 −15.090 1.00 20.58  842 CD1 TYR A 224 49.428 0.464 −13.833 1.00 21.98  843 CD2 TYR A 224 49.429 1.488 −16.013 1.00 22.63  844 CE1 TYR A 224 50.582 1.159 −33.505 1.00 22.51  845 CE2 TYR A 224 50.582 2.386 −15.685 1.00 23.45  846 CZ TYR A 224 51.161 2.018 −14.440 1.00 23.93  847 OH TYR A 224 52.340 2.665 −14.126 1.00 26.78  848 N PRO A 225 44.910 −0.545 −16.957 1.00 23.50  849 CA PRO A 225 45.501 0.350 −37.935 1.00 22.64  850 C PRO A 225 44.900 1.756 −17.867 1.00 22.45  851 O PRO A 225 44.313 2.161 −16.872 1.00 21.99  852 CB PRO A 225 45.385 −0.335 −19.294 1.00 23.11  853 CG PRO A 225 44.382 −1.484 −19.173 1.00 23.73  854 CD PRO A 225 43.979 −1.435 −17.622 1.00 22.80  855 N GLY A 226 45.077 2.458 −19.001 1.00 21.76  856 CA GLY A 226 44.559 3.812 −19.040 1.00 21.93  857 C GLY A 226 43.022 3.923 −19.125 1.00 23.76  858 O GLY A 226 42.405 4.932 −18.809 1.00 23.80  859 N ASN A 227 42.466 2.802 −19.616 1.00 23.49  860 CA ASN A 227 41.038 2.737 −19.670 1.00 24.79  861 C ASN A 227 40.364 1.416 −18.959 1.00 23.66  862 O ASN A 227 41.160 0.489 −18.779 1.00 21.15  863 CB ASN A 227 40.210 2.594 −21.106 1.00 26.98  864 CG ASN A 227 40.485 3.892 −21.877 1.00 29.55  865 OD1 ASN A 227 40.418 4.994 −21.332 1.00 31.48  866 ND2 ASN A 227 40.823 3.724 −23.148 1.00 31.22  867 N ASN A 228 39.094 1.377 −18.571 1.00 23.20  868 CA ASN A 228 38.573 0.197 −17.841 1.00 22.62  869 C ASN A 228 38.683 −1.049 −18.724 1.00 22.14  870 O ASN A 228 38.483 −0.972 −19.949 3.00 21.31  871 CB ASN A 228 37.100 0.435 −17.487 1.00 21.69  872 CG ASN A 228 36.803 1.486 −16.423 3.00 21.12  873 OD1 ASN A 228 35.598 1.769 −16.125 1.00 23.53  874 ND2 ASN A 228 37.794 2.076 −15.831 1.00 18.06  875 N VAL A 229 38.857 −2.232 −18.162 1.00 22.54  876 CA VAL A 229 38.894 −3.464 −18.981 1.00 20.25  877 C VAL A 229 37.524 −4.125 −18.851 1.00 20.80  878 O VAL A 229 37.078 −4.359 −17.734 3.00 20.94  879 CB VAL A 229 39.990 −4.473 −18.584 1.00 19.95  880 CG1 VAL A 229 39.902 −5.773 −19.415 1.00 34.74  881 CG2 VAL A 229 41.389 −3.855 −18.689 1.00 15.89  882 N SER A 230 36.894 −4.469 −19.964 1.00 21.31  883 CA SER A 230 35.595 −5.158 −19.969 1.00 22.94  884 C SER A 230 35.778 −6.674 −19.896 1.00 24.31  885 O SER A 230 36.593 −7.269 −20.616 1.00 21.95  886 CB SER A 230 34.839 −4.769 −23.221 1.00 24.67  887 OG SER A 230 33.548 −5.431 −21.269 1.00 28.19  888 N LEU A 231 35.049 −7.328 −18.993 1.00 24.99  889 CA LEU A 231 35.108 −8.754 −18.760 1.00 26.33  890 C LEU A 231 33.709 −9.391 −18.724 1.00 29.37  891 O LEU A 231 32.966 −9.135 −17.764 1.00 28.67  892 CB LEU A 231 35.779 −9.047 −17.422 1.00 25.50  893 CG LEU A 231 35.803 −10.449 −16.823 1.00 26.01  894 CD1 LEU A 231 36.671 −11.424 −17.607 1.00 25.54  895 CD2 LEU A 231 36.348 −10.425 −15.384 1.00 25.86  896 N THR A 232 33.400 −10.266 −19.692 1.00 30.00  897 CA THR A 232 32.070 −10.894 −19.612 1.00 32.54  898 C THR A 232 32.246 −12.342 −19.188 1.00 32.86  899 O THR A 232 33.069 −13.072 −19.750 1.00 32.67  900 CB THR A 232 31.143 −10.753 −20.806 1.00 33.54  901 OG1 THR A 232 31.043 −11.964 −21.567 1.00 37.56  902 CG2 THR A 232 31.478 −9.607 −21.734 1.00 30.68  903 N VAL A 233 31.540 −12.713 −18.135 1.00 33.79  904 CA VAL A 233 31.579 −14.068 −17.613 1.00 36.22  905 C VAL A 233 30.298 −14.809 −17.947 1.00 38.71  906 O VAL A 233 29.186 −14.331 −17.740 1.00 37.77  907 CB VAL A 233 31.792 −13.955 −16.105 1.00 35.04  908 CG1 VAL A 233 31.838 −15.338 −15.489 1.00 35.88  909 CG2 VAL A 233 33.107 −13.252 −15.847 1.00 33.72  910 N PRO A 234 30.486 −16.031 −18.513 1.00 41.11  911 CA PRO A 234 29.393 −16.841 −19.027 1.00 42.50  912 C PRO A 234 28.491 −17.443 −17.947 1.00 43.33  913 O PRO A 234 28.940 −17.865 −16.889 1.00 45.44  914 CB PRO A 234 29.993 −18.031 −19.783 1.00 41.71  915 CG PRO A 234 31.809 −17.862 −19.793 1.00 42.81  916 CD PRO A 234 31.725 −16.769 −18.640 1.00 42.19  917 N GLN A 235 27.199 −17.504 −18.314 1.00 20.00  918 CA GLN A 235 26.246 −18.000 −17.341 1.00 20.00  919 C GLN A 235 26.543 −19.290 −16.567 1.00 20.00  920 O GLN A 235 26.691 −20.364 −17.135 1.00 20.00  921 CB GLN A 235 24.891 −18.189 −18.091 0.00 20.00  922 CG GLN A 235 23.744 −18.642 −17.182 0.00 20.00  923 CD GLN A 235 22.488 −18.822 −18.002 0.00 20.00  924 OE1 GLN A 235 21.427 −19.185 −17.522 0.00 20.00  925 NE2 GLN A 235 22.653 −18.554 −19.313 0.00 20.00  926 N GLY A 236 26.571 −19.113 −15.235 1.00 20.00  927 CA GLY A 236 26.914 −20.255 −14.411 1.00 20.00  928 C GLY A 236 28.215 −19.843 −13.723 1.00 20.00  929 O GLY A 236 28.571 −20.322 −12.660 1.00 20.00  930 N GLY A 237 28.951 −18.960 −14.432 1.00 45.11  931 CA GLY A 237 30.099 −18.275 −13.853 1.00 43.81  932 C GLY A 237 31.386 −19.060 −14.065 1.00 41.23  933 O GLY A 237 31.412 −20.077 −14.716 1.00 41.47  934 N GLU A 238 32.494 −18.495 −13.570 1.00 39.53  935 CA GLU A 238 33.738 −19.269 −13.544 1.00 36.93  936 C GLU A 238 34.814 −18.623 −12.658 1.00 35.69  937 O GLU A 238 34.687 −17.510 −12.179 1.00 34.73  938 CB GLU A 238 34.249 −19.376 −14.974 1.00 37.46  939 CG GLU A 238 34.152 −18.042 −15.715 1.00 38.60  940 CD GLU A 238 34.928 −18.141 −17.002 1.00 38.06  941 OE1 GLU A 238 36.045 −17.645 −17.053 1.00 39.51  942 OE2 GLU A 238 34.397 −18.708 −17.948 1.00 39.63  943 N LYS A 239 35.917 −19.366 −12.434 1.00 31.34  944 CA LYS A 239 36.752 −18.708 −12.071 1.00 30.50  945 C LYS A 239 38.005 −18.078 −12.734 1.00 29.49  946 O LYS A 239 38.644 −18.729 −13.541 1.00 26.10  947 CB LYS A 239 37.649 −19.635 −11.230 1.00 30.57  948 CG LYS A 239 39.081 −19.338 −10.780 1.00 32.75  949 CD LYS A 239 39.203 −19.871 −9.351 1.00 35.35  950 CE LYS A 239 39.279 −21.314 −8.840 1.00 36.50  951 NZ LYS A 239 39.762 −21.354 −7.46I 1.00 33.54  952 N VAL A 240 38.248 −16.787 −12.495 1.00 26.95  953 CA VAL A 240 39.095 −15.992 −13.399 1.00 23.70  954 C VAL A 240 40.419 −15.640 −12.743 1.00 25.44  955 O VAL A 240 40.437 −15.350 −11.538 1.00 23.90  956 CB VAL A 240 38.369 −14.708 −13.849 1.00 22.65  957 CG1 VAL A 240 39.170 −13.901 −14.866 1.00 22.07  958 CG2 VAL A 240 36.957 −14.947 −14.404 1.00 21.34  959 N THR A 241 41.505 −15.654 −13.524 1.00 24.76  960 CA THR A 241 42.835 −15.308 −13.067 1.00 26.11  961 C THR A 241 43.244 −13.957 −13.689 1.00 26.23  962 O THR A 241 43.165 −13.786 −14.922 1.00 24.94  963 CB THR A 241 43.856 −16.397 −13.451 1.00 26.92  964 OG1 THR A 241 43.594 −17.610 −12.693 1.00 29.26  965 CG2 THR A 241 45.285 −15.969 −13.169 1.00 25.11  966 N PHE A 242 43.659 −13.013 −12.870 1.00 23.69  967 CA PHE A 242 44.060 −11.655 −13.229 1.00 22.06  968 C PHE A 242 45.557 −11.465 −12.984 1.00 22.71  969 O PHE A 242 46.093 −11.901 −11.969 1.00 22.30  970 CB PHE A 242 43.275 −10.648 −12.369 1.00 22.34  971 CG PHE A 242 41.777 −10.695 −12.505 1.00 22.23  972 CD1 PHE A 242 41.137 −9.866 −13.423 1.00 21.94  973 CD2 PHE A 242 40.996 −11.545 −11.747 1.00 22.13  974 CE1 PHE A 242 39.763 −9.870 −13.559 1.00 21.82  975 CE2 PHE A 242 39.622 −11.580 −11.923 1.00 21.18  976 CZ PHE A 242 38.986 −10.744 −12.823 1.00 21.58  977 N THR A 243 46.285 −10.845 −13.922 1.00 20.68  978 CA THR A 243 47.718 −10.737 −13.888 1.00 21.11  979 C THR A 243 48.264 −9.334 −14.094 1.00 21.20  980 O THR A 243 47.787 −8.652 −14.989 1.00 19.64  981 CB THR A 243 48.327 −11.664 −14.974 1.00 22.96  982 OG1 THR A 243 47.919 −13.047 −14.785 1.00 24.34  983 CG2 THR A 243 49.846 −11.654 −14.938 1.00 23.70  984 N TYR A 244 49.357 −8.991 −13.418 1.00 21.69  985 CA TYR A 244 50.053 −7.712 −13.568 1.00 22.20  986 C TYR A 244 51.558 −7.971 −13.653 1.00 22.75  987 O TYR A 244 52.094 −8.753 −12.862 1.00 23.82  988 CB TYR A 244 49.763 −6.781 −12.377 1.00 22.63  989 CG TYR A 244 50.523 −5.466 −12.369 1.00 22.04  990 CD1 TYR A 244 50.308 −4.453 −13.300 1.00 20.84  991 CD2 TYR A 244 51.477 −5.248 −11.386 1.00 22.48  992 CE1 TYR A 244 51.053 −3.287 −13.258 1.00 21.71  993 CE2 TYR A 244 52.175 −4.046 −11.292 1.00 22.10  994 CZ TYR A 244 51.961 −3.071 −12.249 1.00 21.72  995 OH TYR A 244 52.682 −1.888 −12.195 1.00 21.67  996 N ILE A 245 52.258 −7.381 −14.614 1.00 21.91  997 CA ILE A 245 53.672 −7.500 −14.845 1.00 21.21  998 C ILE A 245 54.326 −6.151 −14.564 1.00 22.31  999 O ILE A 245 54.133 −5.163 −15.266 1.00 20.02 1000 CB ILE A 245 53.947 −7.953 −16.298 1.00 22.59 1001 CG1 ILE A 245 53.225 −9.298 −16.560 1.00 23.96 1002 CG2 ILE A 245 55.434 −8.035 −16.554 1.00 18.24 1003 CD1 ILE A 245 53.736 −10.007 −17.795 1.00 27.43 1004 N PRO A 246 54.950 −6.024 −13.382 1.00 23.34 1005 CA PRO A 246 55.533 −4.759 −12.930 1.00 23.67 1006 C PRO A 246 56.505 −4.124 −13.911 1.00 22.46 1007 O PRO A 246 56.416 −2.914 −14.115 1.00 22.69 1008 CB PRO A 246 56.242 −5.151 −11.622 1.00 23.64 1009 CG PRO A 246 55.415 −6.302 −11.119 1.00 22.55 1010 CD PRO A 246 55.177 −7.102 −12.400 1.00 23.30 1011 N SER A 247 57.418 −4.864 −14.543 1.00 21.20 1012 CA SER A 247 58.360 −4.243 −15.475 1.00 23.73 1013 C SER A 247 57.762 −3.511 −16.663 1.00 24.65 1014 O SER A 247 58.401 −2.582 −17.178 1.00 24.40 1015 CB SER A 247 59.408 −5.238 −16.041 1.00 23.42 1016 OG SER A 247 58.758 −6.211 −16.858 1.00 23.25 1017 N THR A 248 56.656 −3.993 −17.221 1.00 23.91 1018 CA THR A 248 56.010 −3.307 −18.332 1.00 23.41 1019 C THR A 248 54.687 −2.652 −17.942 1.00 23.60 1020 O THR A 248 54.054 −1.971 −18.736 1.00 21.55 1021 CB THR A 248 55.680 −4.349 −19.443 1.00 22.17 1022 OG1 THR A 248 54.807 −5.326 −18.855 1.00 17.24 1023 CG2 THR A 248 56.993 −5.005 −19.903 1.00 21.11 1024 N ASN A 249 54.184 −2.889 −15.740 1.00 22.61 1025 CA ASN A 249 52.883 −2.425 −16.291 1.00 22.91 1026 C ASN A 249 51.737 −3.081 −17.080 1.00 20.56 1027 O ASN A 249 50.625 −2.569 −16.955 1.00 20.56 1028 CB ASN A 249 52.698 −0.900 −16.304 1.00 22.75 1029 CG ASN A 249 53.754 −0.182 −15.455 1.00 25.70 1030 OD1 ASN A 249 53.878 −0.393 −14.245 1.00 24.53 1031 ND2 ASN A 249 54.530 0.640 −16.173 1.00 24.05 1032 N GLN A 250 51.886 −4.178 −17.796 1.00 22.09 1033 CA GLN A 250 50.791 −4.759 −18.599 1.00 21.69 1034 C GLN A 250 49.829 −5.589 −17.734 1.00 22.85 1035 O GLN A 250 50.263 −6.152 −16.701 1.00 20.61 1035 CB GLN A 250 51.375 −5.611 −19.720 1.00 22.60 1037 CG GLN A 250 52.265 −4.859 −20.720 1.00 23.80 1038 CD GLN A 250 51.509 −3.725 −21.387 1.00 25.16 1039 OE1 GLN A 250 50.566 −3.959 −22.167 1.00 24.30 1040 NE2 GLN A 250 51.806 −2.490 −20.991 1.00 25.44 1041 N VAL A 251 48.526 −5.568 −18.077 1.00 21.86 1042 CA VAL A 251 47.558 −6.304 −17.262 1.00 21.68 1043 C VAL A 251 46.590 −7.203 −18.149 1.00 21.54 1044 O VAL A 251 46.351 −6.836 −19.273 1.00 19.04 1045 CB VAL A 251 46.580 −5.498 −16.291 1.00 23.56 1046 CG1 VAL A 251 47.093 −4.039 −16.093 1.00 22.08 1047 CG2 VAL A 251 45.175 −5.587 −16.451 1.00 22.66 1048 N PHE A 252 46.486 −8.436 −17.687 1.00 20.51 1049 CA PHE A 252 45.764 −9.449 −18.458 1.00 21.29 1050 C PHE A 252 44.747 −10.183 −17.592 1.00 22.46 1051 O PHE A 252 44.936 −10.267 −16.368 1.00 24.63 1052 CB PHE A 252 46.763 −10.520 −18.984 1.00 18.87 1053 CG PHE A 252 47.927 −9.918 −19.740 1.00 19.77 1054 CD1 PHE A 252 47.771 −9.602 −21.089 1.00 19.15 1055 CD2 PHE A 252 49.087 −9.536 −19.076 1.00 19.82 1056 CE1 PHE A 252 48.807 −9.007 −21.784 1.00 18.25 1057 CE2 PHE A 252 50.125 −8.926 −19.777 1.00 21.04 1058 CZ PHE A 252 49.981 −8.666 −21.127 1.00 19.76 1059 N ASP A 253 43.766 −10.823 −18.207 1.00 21.21 1060 CA ASP A 253 42.883 −11.739 −17.490 1.00 21.71 1061 C ASP A 253 42.766 −13.015 −18.357 1.00 23.08 1062 O ASP A 253 42.922 −12.971 −19.582 1.00 20.43 1063 CB ASP A 253 41.525 −11.192 −17.091 1.00 22.08 1064 CG ASP A 253 40.668 −10.833 −18.296 1.00 23.51 1065 OD1 ASP A 253 40.153 −11.833 −18.864 1.00 23.59 1066 OD2 ASP A 253 40.550 −9.643 −18.650 1.00 22.42 1067 N SER A 254 42.493 −14.153 −17.717 1.00 21.89 1068 CA SER A 254 42.414 −15.435 −18.370 1.00 23.57 1069 C SER A 254 41.210 −15.586 −19.294 1.00 25.86 1070 O SER A 254 41.180 −16.566 −20.049 1.00 25.58 1071 CB SER A 254 42.435 −16.597 −17.360 1.00 23.34 1072 OG SER A 254 41.247 −16.555 −16.579 1.00 24.91 1073 N VAL A 255 40.213 −14.721 −19.243 1.00 26.09 1074 CA VAL A 255 39.076 −14.799 −20.148 1.00 28.53 1075 C VAL A 255 39.390 −14.071 −21.453 1.00 27.79 1076 O VAL A 255 39.341 −14.648 −22.555 1.00 26.52 1077 CB VAL A 255 37.816 −14.186 −19.501 1.00 30.76 1078 CG1 VAL A 255 36.638 −14.033 −20.441 1.00 31.26 1079 CG2 VAL A 255 37.385 −14.972 −18.275 1.00 31.36 1080 N ASN A 256 39.792 −12.806 −21.335 1.00 25.55 1081 CA ASN A 256 40.178 −12.043 −22.536 1.00 25.41 1082 C ASN A 256 41.509 −12.509 −23.144 1.00 27.70 1083 O ASN A 256 41.629 −12.355 −24.377 1.00 26.77 1084 CB ASN A 256 40.271 −10.550 −22.246 1.00 24.63 1085 CG ASN A 256 38.942 −9.900 −21.914 1.00 24.57 1086 OD1 ASN A 256 38.017 −9.952 −22.712 1.00 24.02 1087 ND2 ASN A 256 38.809 −9.279 −20.740 1.00 26.72 1088 N HIS A 257 42.432 −13.073 −22.365 1.00 25.02 1089 CA HIS A 257 43.727 −13.532 −22.914 1.00 26.70 1090 C HIS A 257 44.127 −14.879 −22.303 1.00 25.24 1091 O HIS A 257 44.864 −14.982 −21.322 1.00 22.57 1092 CB HIS A 257 44.801 −12.505 −22.514 1.00 27.64 1093 CG HIS A 257 46.027 −12.421 −23.350 1.00 31.69 1094 ND1 HIS A 257 46.809 −13.517 −23.674 1.00 33.57 1095 CD2 HIS A 257 46.623 −11.354 −23.934 1.00 31.77 1096 CE1 HIS A 257 47.830 −13.122 −24.433 1.00 34.40 1097 NE2 HIS A 257 47.743 −11.807 −24.598 1.00 34.33 1098 N PRO A 258 43.641 −15.986 −22.850 1.00 26.17 1099 CA PRO A 258 43.867 −17.303 −22.260 1.00 26.23 1100 C PRO A 258 45.227 −17.896 −22.590 1.00 26.44 1101 O PRO A 258 45.420 −18.723 −23.495 1.00 24.80 1102 CB PRO A 258 42.694 −18.124 −22.806 1.00 27.73 1103 CG PRO A 258 42.303 −17.456 −24.089 1.00 27.71 1104 CD PRO A 258 42.602 −15.992 −23.915 1.00 25.96 1105 N ASN A 259 46.254 −17.533 −21.821 1.00 26.95 1106 CA ASN A 259 47.623 −18.021 −21.925 1.00 25.18 1107 C ASN A 259 48.347 −17.710 −20.611 1.00 25.96 1108 O ASN A 259 48.451 −16.546 −20.208 1.00 26.02 1109 CB ASN A 259 48.371 −17.392 −23.103 1.00 25.42 1110 CG ASN A 259 49.814 −17.787 −23.316 1.00 25.25 1111 OD1 ASN A 259 50.440 −17.469 −24.364 1.00 28.24 1112 ND2 ASN A 259 50.464 −18.457 −22.388 1.00 23.35 1113 N GLN A 260 48.760 −18.771 −19.919 1.00 25.82 1114 CA GLN A 260 49.491 −18.660 −18.660 1.00 24.61 1115 C GLN A 260 50.983 −18.858 −18.828 1.00 25.53 1116 O GLN A 260 51.682 −18.938 −17.782 1.00 26.85 1117 CB GLN A 260 48.992 −19.714 −17.639 1.00 22.83 1118 CG GLN A 260 47.560 −19.480 −17.212 1.00 23.92 1119 CD GLN A 260 47.324 −18.192 −16.433 1.00 24.42 1120 OE1 GLN A 260 47.977 −17.871 −15.455 1.00 22.77 1121 NE2 GLN A 260 46.320 −17.451 −16.908 1.00 24.04 1122 N ALA A 261 51.524 −18.902 −20.070 1.00 24.54 1123 CA ALA A 261 52.993 −19.039 −20.165 1.00 24.10 1124 C ALA A 261 53.724 −17.709 −19.962 1.00 23.98 1125 O ALA A 261 54.494 −17.243 −20.832 1.00 22.89 1126 CB ALA A 261 53.400 −19.687 −21.497 1.00 22.32 1127 N PHE A 262 53.543 −17.054 −18.836 1.00 24.03 1128 CA PHE A 262 54.150 −15.787 −18.465 1.00 24.14 1129 C PHE A 262 55.652 −15.897 −18.208 1.00 25.13 1130 O PHE A 262 56.198 −16.920 −17.778 1.00 23.35 1131 CB PHE A 262 53.411 −15.253 −17.213 1.00 22.37 1132 CG PHE A 262 52.022 −14.753 −17.488 1.00 22.59 1133 CD1 PHE A 262 50.911 −15.437 −17.022 1.00 22.84 1134 CD2 PHE A 262 51.816 −13.575 −18.202 1.00 22.43 1135 CE1 PHE A 262 49.624 −14.989 −17.269 1.00 21.45 1136 CE2 PHE A 262 50.541 −13.133 −18.472 1.00 22.97 1137 CZ PHE A 262 49.440 −13.813 −18.003 1.00 22.36 1138 N PRO A 263 56.379 −14.800 −18.443 1.00 25.77 1139 CA PRO A 263 57.810 −14.746 −18.276 1.00 27.78 1140 C PRO A 263 58.230 −14.812 −16.809 1.00 29.38 1141 O PRO A 263 57.444 −14.598 −15.893 1.00 26.79 1142 CB PRO A 263 58.220 −13.454 −18.976 1.00 27.35 1143 CG PRO A 263 57.026 −12.629 −19.136 1.00 25.87 1144 CD PRO A 263 55.836 −13.514 −18.913 1.00 27.36 1145 N THR A 264 59.466 −15.244 −16.602 1.00 31.59 1146 CA THR A 264 60.041 −15.460 −15.284 1.00 34.76 1147 C THR A 264 61.224 −14.566 −14.986 1.00 35.79 1148 O THR A 264 61.745 −14.682 −13.867 1.00 37.84 1149 CB THR A 264 60.547 −16.920 −15.177 1.00 35.70 1150 OG1 THR A 264 61.354 −17.199 −16.330 1.00 37.91 1151 CG2 THR A 264 59.441 −17.952 −15.205 1.00 36.80 1152 N SER A 265 61.739 −13.812 −15.944 1.00 35.41 1153 CA SER A 265 62.935 −13.002 −15.805 1.00 36.21 1154 C SER A 265 62.656 −11.549 −15.439 1.00 37.19 1155 O SER A 265 61.609 −10.978 −15.750 1.00 38.21 1156 CB SER A 265 63.740 −13.074 −17.100 1.00 36.57 1157 OG SER A 265 64.697 −12.050 −17.291 1.00 35.80 1155 N SER A 266 63.601 −10.915 −14.750 1.00 35.57 1155 CA SER A 266 63.488 −9.539 −14.271 1.00 34.73 1160 C SER A 266 64.355 −8.615 −15.113 1.00 35.65 1161 O SER A 266 64.631 −7.441 −14.841 1.00 33.89 1162 CB SER A 266 63.830 −9.438 −12.779 1.00 33.46 1163 OG SER A 266 62.821 −10.053 −11.983 1.00 33.15 1164 N ALA A 267 64.865 −9.185 −16.221 1.00 36.92 1165 CA ALA A 267 65.657 −8.374 −17.145 1.00 38.86 1166 C ALA A 267 64.766 −7.194 −17.577 1.00 40.22 1167 O ALA A 267 63.560 −7.315 −17.771 1.00 38.69 1168 CB ALA A 267 66.132 −9.162 −18.339 1.00 39.06 1169 N GLY A 268 65.403 −6.030 −17.573 1.00 42.28 1170 CA GLY A 268 64.752 −4.784 −17.865 1.00 44.37 1171 C GLY A 268 64.348 −3.978 −16.643 1.00 46.77 1172 O GLY A 268 64.299 −2.737 −16.795 1.00 47.62 1173 N VAL A 269 64.052 −4.595 −15.480 1.00 46.24 1174 CA VAL A 269 63.594 −3.736 −14.385 1.00 45.82 1175 C VAL A 269 64.666 −2.835 −13.801 1.00 44.79 1176 O VAL A 269 65.871 −3.071 −13.802 1.00 44.61 1177 CB VAL A 269 62.762 −4.389 −13.300 1.00 47.26 1178 CG1 VAL A 269 61.276 −4.187 −13.663 1.00 47.77 1179 CG2 VAL A 269 62.947 −5.864 −13.074 1.00 47.82 1180 N GLN A 270 64.168 −1.666 −13.364 1.00 44.38 1181 CA GLN A 270 65.117 −0.651 −12.866 1.00 43.41 1182 C GLN A 270 65.016 −0.541 −11.348 1.00 39.99 1183 O GLN A 270 63.909 −0.536 −10.823 1.00 39.03 1184 CB GLN A 270 64.909 0.628 −13.663 1.00 44.70 1185 CG GLN A 270 63.545 1.259 −13.564 1.00 46.40 1186 CD GLN A 270 63.594 2.718 −14.049 1.00 48.21 1187 OE1 GLN A 270 63.352 3.648 −13.263 1.00 49.65 1188 NE2 GLN A 270 63.949 2.916 −15.320 1.00 47.11 1189 N THR A 271 66.168 −0.620 −10.661 1.00 36.93 1190 CA THR A 271 66.136 −0.641 −9.198 1.00 32.17 1191 C THR A 271 67.457 −0.271 −8.565 1.00 31.16 1192 O THR A 271 68.558 −0.403 −9.078 1.00 29.69 1193 CB THR A 271 65.681 −2.033 −8.683 1.00 32.24 1194 OG1 THR A 271 65.608 −2.075 −7.243 1.00 30.97 1195 CG2 THR A 271 66.584 −3.179 −9.133 1.00 30.31 1196 N ASN A 272 67.330 0.245 −7.332 1.00 28.98 1197 CA ASN A 272 68.481 0.558 −6.529 1.00 26.71 1198 C ASN A 272 68.527 −0.399 −5.322 1.00 24.87 1199 O ASN A 272 69.417 −0.272 −4.515 1.00 22.11 1200 CB ASN A 272 68.464 2.031 −6.162 1.00 27.42 1201 CG ASN A 272 67.423 2.457 −5.152 1.00 27.32 1202 OD1 ASN A 272 67.473 3.640 −4.735 1.00 28.32 1203 ND2 ASN A 272 66.516 1.631 −4.751 1.00 25.56 1204 N LEU A 273 67.770 −1.488 −5.320 1.00 24.32 1205 CA LEU A 273 67.740 −2.431 −4.206 1.00 24.89 1206 C LEU A 273 67.477 −3.819 −4.758 1.00 24.94 1207 O LEU A 273 66.401 −4.035 −5.326 1.00 23.57 1208 CB LEU A 273 66.640 −2.010 −3.197 1.00 25.97 1209 CG LEU A 273 66.566 −2.816 −1.893 1.00 24.77 1210 CD1 LEU A 273 67.763 −2.539 −0.981 1.00 23.86 1211 CD2 LEU A 273 65.279 −2.514 −1.136 1.00 25.15 1212 N VAL A 274 68.455 −4.706 −4.675 1.00 24.94 1213 CA VAL A 274 68.417 −5.999 −5.341 1.00 26.05 1214 C VAL A 274 68.515 −7.184 −4.379 1.00 26.04 1215 O VAL A 274 69.229 −7.097 −3.381 1.00 26.70 1216 CB VAL A 274 69.583 −6.171 −6.361 1.00 25.86 1217 CG1 VAL A 274 69.620 −5.082 −7.432 1.00 25.76 1218 CG2 VAL A 274 70.921 −6.116 −5.640 1.00 26.10 1219 N GLN A 275 67.836 −8.261 −4.692 1.00 25.69 1220 CA GLN A 275 67.948 −9.534 −4.016 1.00 27.38 1221 C GLN A 275 68.722 −10.509 −4.924 1.00 26.18 1222 O GLN A 275 68.335 −10.671 −6.064 1.00 24.99 1223 CB GLN A 275 66.596 −10.143 −3.662 1.00 26.97 1224 CG GLN A 275 66.671 −11.477 −2.930 1.00 28.59 1225 CD GLN A 275 65.265 −11.964 −2.607 1.00 32.32 1226 OE1 GLN A 275 64.501 −11.303 −1.895 1.00 33.16 1227 NE2 GLN A 275 64.893 −13.118 −3.136 1.00 32.96 1228 N LEU A 276 69.837 −11.012 −4.427 1.00 25.42 1229 CA LEU A 276 70.697 −11.944 −5.130 1.00 25.50 1230 C LEU A 276 70.562 −13.358 −4.573 1.00 26.02 1231 O LEU A 276 70.448 −13.492 −3.342 1.00 26.72 1232 CB LEU A 276 72.157 −11.498 −5.051 1.00 23.09 1233 CG LEU A 276 72.473 −10.046 −5.406 1.00 24.38 1234 CD1 LEU A 276 73.930 −9.640 −5.129 1.00 23.10 1235 CD2 LEU A 276 72.173 −9.799 −6.886 1.00 22.76 1236 N THR A 277 70.615 −14.370 −5.434 1.00 25.00 1237 CA THR A 277 70.574 −15.758 −5.009 1.00 24.89 1238 C THR A 277 71.967 −16.301 −5.329 1.00 25.72 1239 O THR A 277 72.476 −15.942 −6.401 1.00 26.30 1240 CB THR A 277 69.479 −16.586 −5.694 1.00 27.01 1241 OG1 THR A 277 68.199 −15.975 −5.436 1.00 27.31 1242 CG2 THR A 277 69.423 −18.028 −5.179 1.00 25.75 1243 N LEU A 278 72.567 −17.086 −4.445 1.00 24.33 1244 CA LEU A 278 73.924 −17.581 −4.635 1.00 24.69 1245 C LEU A 278 73.883 −19.074 −4.953 1.00 25.40 1246 O LEU A 278 72.925 −19.707 −4.513 1.00 25.92 1247 CB LEU A 278 74.755 −17.375 −3.349 1.00 24.44 1248 CG LEU A 278 74.785 −15.959 −2.779 1.00 25.93 1249 CD1 LEU A 278 75.676 −15.830 −1.528 1.00 25.09 1250 CD2 LEU A 278 75.228 −14.960 −3.842 1.00 25.13 1251 N ALA A 279 74.866 −19.602 −5.666 1.00 25.25 1252 CA ALA A 279 74.847 −21.038 −5.956 1.00 27.68 1253 C ALA A 279 75.156 −21.861 −4.701 1.00 26.75 1254 O ALA A 279 74.770 −23.030 −4.671 1.00 25.73 1255 CB ALA A 279 75.804 −21.373 −7.095 1.00 27.60 1256 N SER A 280 75.918 −21.347 −3.736 1.00 26.02 1257 CA SER A 280 76.117 −22.146 −2.509 1.00 28.04 1258 C SER A 280 76.067 −21.219 −1.293 1.00 27.40 1259 O SER A 280 76.144 −19.994 −1.449 1.00 27.94 1260 CB SER A 280 77.417 −22.948 −2.579 1.00 27.93 1261 OG SER A 280 78.501 −22.049 −2.693 1.00 27.71 1262 N ALA A 281 76.919 −21.724 −0.101 1.00 26.67 1263 CA ALA A 281 75.824 −20.907 1.108 1.00 26.36 1264 C ALA A 281 77.169 −20.545 1.709 1.00 26.18 1265 O ALA A 281 77.935 −21.377 2.183 1.00 25.41 1266 CB ALA A 281 75.004 −21.696 2.132 1.00 26.66 1267 N PRO A 282 77.452 −19.248 1.797 1.00 27.13 1268 CA PRO A 282 78.677 −18.742 2.392 1.00 27.03 1269 C PRO A 282 78.792 −19.115 3.866 1.00 26.41 1270 O PRO A 282 77.776 −19.312 4.518 1.00 24.07 1271 CB PRO A 282 78.587 −17.226 2.229 1.00 26.76 1272 CG PRO A 282 77.126 −16.962 2.093 1.00 28.81 1273 CD PRO A 282 76.589 −18.131 1.316 1.00 27.00 1274 N ASP A 283 80.031 −19.217 4.332 1.00 24.52 1276 CA ASP A 283 80.333 −19.422 5.754 1.00 24.81 1276 C ASP A 283 80.147 −18.073 6.436 1.00 22.38 1277 O ASP A 283 80.864 −17.107 6.145 1.00 21.69 1278 CB ASP A 283 81.775 −19.935 5.887 1.00 26.32 1279 CG ASP A 283 82.210 −20.254 7.297 1.00 26.30 1280 OD1 ASP A 283 82.960 −21.237 7.484 1.00 25.14 1281 OD2 ASP A 283 81.801 −19.636 8.239 1.00 26.29 1282 N VAL A 284 79.206 −17.940 7.380 1.00 22.67 1283 CA VAL A 284 78.952 −16.654 8.036 1.00 22.22 1284 C VAL A 284 80.074 −16.100 8.887 1.00 24.46 1285 O VAL A 284 80.021 −14.907 9.268 1.00 24.83 1286 CB VAL A 284 77.642 −16.672 8.867 1.00 22.56 1287 CG1 VAL A 284 76.463 −17.083 7.976 1.00 19.20 1288 CG2 VAL A 284 77.712 −17.517 10.125 1.00 19.74 1289 N THR A 285 81.154 −16.864 9.118 1.00 22.48 1290 CA THR A 285 82.292 −16.304 9.840 1.00 22.60 1291 C THR A 285 83.379 −15.770 8.912 1.00 22.76 1292 O THR A 285 84.414 −15.336 9.433 1.00 23.50 1293 CB THR A 285 82.906 −17.394 10.742 1.00 22.23 1294 OG1 THR A 285 83.613 −18.376 9.942 1.00 22.05 1295 CG2 THR A 285 81.829 −18.132 11.629 1.00 19.25 1296 N HIS A 286 83.257 −15.892 7.608 1.00 23.16 1297 CA HIS A 286 84.273 −15.462 6.656 1.00 24.10 1298 C HIS A 286 84.119 −14.015 6.202 1.00 23.79 1299 O HIS A 286 83.119 −13.382 6.557 1.00 20.85 1300 CB HIS A 286 84.336 −16.407 5.450 1.00 25.64 1301 CG HIS A 286 85.025 −17.700 5.781 1.00 26.97 1302 ND1 HIS A 286 85.197 −18.702 4.857 1.00 27.65 1303 CD2 HIS A 286 85.496 −18.195 6.960 1.00 27.96 1304 CE1 HIS A 286 85.827 −19.731 6.390 1.00 27.73 1305 NE2 HIS A 286 86.003 −19.451 6.664 1.00 29.50 1306 N ASN A 287 85.074 −13.467 6.472 1.00 23.23 1307 CA ASN A 287 85.032 −12.068 5.021 1.00 26.78 1308 C ASN A 287 84.421 −12.025 3.625 1.00 26.70 1309 O ASN A 287 86.103 −12.453 2.685 1.00 26.28 1310 CB ASN A 287 86.459 −11.491 4.965 1.00 29.01 1311 CG ASN A 287 86.508 −10.068 4.447 1.00 30.90 1312 OD1 ASN A 287 85.568 −9.293 4.561 1.00 31.63 1313 ND2 ASN A 287 87.625 −9.643 3.861 1.00 32.44 1314 N LEU A 288 83.160 −11.657 3.461 1.00 25.67 1315 CA LEU A 288 82.489 −11.815 2.175 1.00 25.40 1316 C LEU A 288 82.186 −10.519 1.449 1.00 26.63 1317 O LEU A 288 81.657 −9.651 2.046 1.00 26.44 1318 CB LEU A 288 81.178 −12.587 2.402 1.00 24.27 1319 CG LEU A 288 81.261 −13.809 3.317 1.00 24.67 1320 CD1 LEU A 288 79.857 −14.127 3.887 1.00 26.43 1321 CD2 LEU A 288 81.787 −15.040 2.602 1.00 24.91 1322 N ASP A 289 82.647 −10.462 0.170 1.00 26.00 1323 CA ASP A 289 82.295 −9.192 −0.541 1.00 28.88 1324 C ASP A 289 81.371 −9.408 −1.731 1.00 26.48 1325 O ASP A 289 81.368 −10.484 −2.310 1.00 26.03 1326 CB ASP A 289 83.633 −8.684 −0.986 1.00 33.27 1327 CG ASP A 289 84.133 −7.466 −0.104 1.00 36.80 1328 OD1 ASP A 289 83.766 −7.242 1.063 1.00 38.78 1329 OD2 ASP A 289 84.979 −6.701 −0.626 1.00 40.62 1330 N VAL A 290 80.617 −8.385 −2.091 1.00 26.24 1331 CA VAL A 290 79.774 −8.372 −3.271 1.00 25.70 1332 C VAL A.290 80.162 −7.119 −4.086 1.00 27.14 1333 O VAL A 290 80.498 −6.084 −3.527 1.00 26.07 1334 CB VAL A 290 78.259 −8.332 −2.999 1.00 24.55 1335 CG1 VAL A 290 77.827 −7.147 −2.128 1.00 22.41 1336 CG2 VAL A 290 77.423 −8.332 −4.289 1.00 23.49 1337 N ALA A 291 80.104 −7.252 −5.408 1.00 29.18 1338 CA ALA A 291 80.361 −6.141 −6.312 1.00 30.04 1339 C ALA A 291 79.519 −6.327 −7.579 1.00 30.92 1340 O ALA A 291 78.916 −7.386 −7.813 1.00 29.72 1341 CB ALA A 291 81.857 −6.093 −6.675 1.00 29.98 1342 N ALA A 292 79.485 −5.297 −8.406 1.00 33.04 1343 CA ALA A 292 78.809 −5.359 −9.703 1.00 34.88 1344 C ALA A 292 79.590 −4.566 −10.738 1.00 36.66 1345 O ALA A 292 80.342 −3.645 −10.375 1.00 36.13 1346 CB ALA A 292 77.395 −4.832 −9.570 1.00 35.02 1347 N ASP A 293 79.430 −4.891 −12.019 1.00 39.96 1348 CA ASP A 293 80.165 −4.141 −13.054 1.00 42.63 1349 C ASP A 293 79.890 −2.644 −12.977 1.00 41.11 1350 O ASP A 293 78.750 −2.184 −13.100 1.00 41.97 1351 CB ASP A 293 79.817 −4.670 −14.451 1.00 46.42 1352 CG ASP A 293 80.532 −3.867 −15.535 1.00 49.75 1353 OD1 ASP A 293 81.775 −3.978 −15.683 1.00 50.50 1354 OD2 ASP A 293 79.821 −3.106 −16.246 1.00 51.35 1355 N GLY A 294 80.904 −1.835 −12.717 1.00 40.88 1356 CA GLY A 294 80.737 −0.390 −12.588 1.00 41.91 1357 C GLY A 294 80.525 0.114 −11.170 1.00 41.98 1358 O GLY A 294 80.616 1.353 −10.921 1.00 42.78 1359 N TYR A 295 80.314 −0.798 −10.204 1.00 39.89 1360 CA TYR A 295 80.112 −0.393 −8.813 1.00 38.42 1361 C TYR A 295 81.240 −0.871 −7.900 1.00 37.45 1362 O TYR A 295 81.573 −2.057 −7.972 1.00 38.33 1363 CB TYR A 295 78.808 −0.951 −8.238 1.00 36.42 1364 CG TYR A 295 77.510 −0.422 −8.776 1.00 35.08 1365 CD1 TYR A 295 76.787 0.576 −8.131 1.00 33.65 1366 CD2 TYR A 295 77.014 −0.921 −9.988 1.00 34.53 1367 CE1 TYR A 295 75.587 1.055 −8.644 1.00 32.54 1368 CE2 TYR A 295 75.851 −0.409 −10.548 1.00 33.98 1369 CZ TYR A 295 75.142 0.565 −9.856 1.00 33.30 1370 OH TYR A 295 73.963 1.007 −10.411 1.00 31.85 1371 N LYS A 296 81.795 −0.014 −7.051 1.00 36.68 1372 CA LYS A 296 82.757 −0.537 −6.079 1.00 36.58 1373 C LYS A 296 82.057 −1.439 −5.060 1.00 34.22 1374 O LYS A 296 80.894 −1.258 −4.694 1.00 31.79 1375 CB LYS A 296 83.624 0.497 −5.430 1.00 39.77 1376 CG LYS A 296 83.045 1.710 −4.813 1.00 43.12 1377 CD LYS A 296 82.983 1.676 −3.283 1.00 45.75 1378 CE LYS A 296 84.388 1.604 −2.699 1.00 47.63 1379 NZ LYS A 296 84.818 0.148 −2.669 1.00 48.54 1380 N ALA A 297 82.840 −2.431 −4.652 1.00 30.70 1381 CA ALA A 297 82.424 −3.491 −3.761 1.00 28.61 1382 C ALA A 297 82.078 −3.124 −2.319 1.00 28.36 1383 O ALA A 297 82.475 −2.094 −1.762 1.00 24.23 1384 CB ALA A 297 83.576 −4.498 −3.796 1.00 28.17 1385 N HIS A 298 81.359 −4.049 −1.654 1.00 25.58 1386 CA HIS A 298 81.044 −3.900 −0.241 1.00 25.55 1387 C HIS A 298 81.031 −5.260 0.470 1.00 22.74 1388 O HIS A 298 80.656 −6.242 −0.135 1.00 23.46 1389 CB HIS A 298 79.678 −3.242 −0.038 1.00 25.93 1390 CG HIS A 298 79.409 −2.728 1.343 1.00 24.84 1391 ND1 HIS A 298 79.527 −1.366 1.547 1.00 25.94 1392 CD2 HIS A 298 79.039 −3.239 2.536 1.00 22.97 1393 CE1 HIS A 298 79.249 −1.045 2.793 1.00 24.28 1394 NE2 HIS A 298 78.944 −2.172 3.412 1.00 23.71 1395 N ASN A 299 81.383 −5.265 1.739 1.00 22.36 1396 CA ASN A 299 81.334 −6.364 2.665 1.00 22.13 1397 C ASN A 299 79.897 −6.847 2.839 1.00 20.98 1398 O ASN A 299 78.992 −6.014 2.842 1.00 17.58 1399 CB ASN A 299 81.878 −5.915 4.056 1.00 22.29 1400 CG ASN A 299 81.745 −7.085 5.033 1.00 22.68 1401 OD1 ASN A 299 82.457 −8.091 4.922 1.00 23.89 1402 ND2 ASN A 299 80.826 −6.978 5.967 1.00 22.28 1403 N ILE A 300 79.663 −8.134 2.970 1.00 19.88 1404 CA ILE A 300 78.342 −8.681 3.200 1.00 21.29 1405 C ILE A 300 78.204 −9.065 4.694 1.00 20.22 1406 O ILE A 300 78.956 −9.925 5.183 1.00 20.11 1407 CB ILE A 300 78.053 −9.924 2.344 1.00 20.62 1408 CG1 ILE A 300 78.330 −9.621 0.866 1.00 21.23 1409 CG2 ILE A 300 76.614 −10.380 2.533 1.00 21.02 1410 CD1 ILE A 300 78.258 −10.831 −0.021 1.00 20.37 1411 N LEU A 301 77.336 −8.388 5.423 1.00 17.75 1412 CA LEU A 301 77.209 −8.699 6.870 1.00 18.06 1413 C LEU A 301 76.024 −9.630 7.119 1.00 17.18 1414 O LEU A 301 74.921 −9.397 6.603 1.00 15.63 1415 CB LEU A 301 77.007 −7.399 7.657 1.00 17.96 1416 CG LEU A 301 77.055 −7.516 9.198 1.00 19.15 1417 CD1 LEU A 301 78.494 −7.470 9.695 1.00 17.41 1418 CD2 LEU A 301 76.236 −6.376 9.814 1.00 17.81 1419 N PRO A 302 76.217 −10.719 7.848 1.00 15.47 1420 CA PRO A 302 75.088 −11.614 8.092 1.00 15.32 1421 C PRO A 302 74.052 −10.972 9.021 1.00 15.88 1422 O PRO A 302 74.372 −10.349 10.023 1.00 16.78 1423 CB PRO A 302 75.628 −12.891 8.738 1.00 14.74 1424 CG PRO A 302 77.150 −12.804 8.778 1.00 16.15 1425 CD PRO A 302 77.395 −11.247 8.517 1.00 15.56 1426 N ARG A 303 72.765 −11.115 8.636 1.00 14.90 1427 CA ARG A 303 71.700 −10.524 9.441 1.00 14.86 1428 C ARG A 303 70.536 −11.502 9.653 1.00 12.98 1429 O ARG A 303 70.394 −12.126 10.696 1.00 12.86 1430 CB ARG A 303 71.204 −9.270 8.718 1.00 15.19 1431 CG ARG A 303 69.950 −8.675 9.361 1.00 15.51 1432 CD ARG A 303 69.519 −7.377 8.675 1.00 16.61 1433 NE ARG A 303 68.772 −7.664 7.445 1.00 17.37 1434 CZ ARG A 303 67.916 −6.721 7.011 1.00 19.59 1435 NH1 ARG A 303 67.775 −5.593 7.686 1.00 18.10 1436 NH2 ARG A 303 67.226 −6.920 5.887 1.00 17.39 1437 N ASN A 304 69.665 −11.600 8.626 1.00 14.70 1438 CA ASN A 304 68.496 −12.476 8.741 1.00 14.47 1439 C ASN A 304 68.829 −13.961 8.551 1.00 15.73 1440 O ASN A 304 68.090 −14.850 8.955 1.00 16.46 1441 CB ASN A 304 67.423 −12.026 7.748 1.00 14.98 1442 CG ASN A 304 66.623 −10.906 8.362 1.00 15.04 1443 OD1 ASN A 304 66.852 −10.495 9.494 1.00 16.92 1444 ND2 ASN A 304 65.660 −10.396 7.575 1.00 14.95 1445 N VAL A 305 69.997 −14.272 8.008 1.00 15.65 1446 CA VAL A 305 70.457 −15.659 7.877 1.00 15.60 1447 C VAL A 305 70.641 −16.261 9.281 1.00 14.99 1448 O VAL A 305 70.346 −17.453 9.542 1.00 13.78 1449 CB VAL A 305 71.763 −15.754 7.057 1.00 16.12 1450 CG1 VAL A 305 72.886 −15.007 7.820 1.00 16.01 1451 CG2 VAL A 305 72.211 −17.204 6.923 1.00 14.70 1452 N LEU A 306 70.943 −15.455 10.302 1.00 15.35 1453 CA LEU A 306 71.061 −15.925 11.682 1.00 16.85 1454 C LEU A 306 69.742 −16.291 12.359 1.00 16.79 1455 O LEU A 306 69.821 −16.866 13.444 1.00 16.11 1456 CB LEU A 306 71.854 −14.947 12.574 1.00 17.30 1457 CG LEU A 306 73.183 −14.497 11.943 1.00 18.98 1458 CD1 LEU A 306 73.755 −13.292 12.719 1.00 21.71 1459 CD2 LEU A 306 74.171 −15.623 11.853 1.00 17.50 1460 N ASN A 307 68.579 −16.074 11.742 1.00 17.17 1461 CA ASN A 307 67.295 −16.537 12.219 1.00 19.40 1462 C ASN A 307 67.118 −18.065 11.996 1.00 22.23 1463 O ASN A 307 66.235 −18.629 12.645 1.00 19.61 1464 CB ASN A 307 66.072 −15.914 11.520 1.00 17.50 1465 CG ASN A 307 65.952 −14.411 11.499 1.00 19.19 1466 OD1 ASN A 307 66.604 −13.703 12.268 1.00 16.40 1467 ND2 ASN A 307 65.093 −13.861 10.615 1.00 16.76 1468 N LEU A 308 67.846 −18.698 11.079 1.00 20.99 1469 CA LEU A 308 67.709 −20.121 10.793 1.00 20.83 1470 C LEU A 308 67.998 −21.006 11.995 1.00 21.03 1471 O LEU A 308 68.784 −20.723 12.906 1.00 18.48 1472 CB LEU A 308 68.641 −20.561 9.636 1.00 21.47 1473 CG LEU A 308 68.405 −19.861 8.291 1.00 23.03 1474 CD1 LEU A 308 69.489 −20.134 7.261 1.00 23.09 1475 CD2 LEU A 308 67.039 −20.248 7.739 1.00 21.71 1476 N PRO A 309 67.320 −22.166 12.049 1.00 20.22 1477 CA PRO A 309 67.416 −23.095 13.161 1.00 19.80 1478 C PRO A 309 68.812 −23.561 13.507 1.00 19.00 1479 O PRO A 309 69.113 −23.663 14.715 1.00 19.17 1480 CB PRO A 309 66.476 −24.256 12.793 1.00 20.37 1481 CG PRO A 309 65.446 −23.573 11.949 1.00 19.19 1482 CD PRO A 309 66.282 −22.609 11.100 1.00 19.26 1483 N ARG A 310 69.744 −23.653 12.564 1.00 18.57 1484 CA ARG A 310 71.114 −24.027 12.882 1.00 18.99 1485 C ARG A 310 71.813 −23.033 13.806 1.00 20.10 1486 O ARG A 310 72.758 −23.400 14.544 1.00 19.39 1487 CB ARG A 310 71.910 −24.244 11.582 1.00 21.29 1488 CG ARG A 310 72.315 −22.947 10.876 1.00 23.49 1489 CD ARG A 310 73.173 −23.235 9.648 1.00 25.45 1490 NE ARG A 310 74.564 −23.436 10.024 1.00 30.55 1491 CZ ARG A 310 75.583 −23.674 9.187 1.00 33.31 1492 NH1 ARG A 310 75.463 −23.744 7.854 1.00 33.05 1493 NH2 ARG A 310 76.793 −23.814 9.703 1.00 33.33 1494 N TYR A 311 71.378 −21.761 13.838 1.00 18.74 1495 CA TYR A 311 71.933 −20.818 14.800 1.00 19.14 1496 C TYR A 311 71.067 −20.575 16.024 1.00 19.76 1497 O TYR A 311 71.260 −19.550 16.682 1.00 19.20 1498 CB TYR A 311 72.119 −19.454 14.074 1.00 20.52 1499 CG TYR A 311 72.939 −19.630 12.795 1.00 20.06 1500 CD1 TYR A 311 72.341 −19.445 11.558 1.00 19.78 1501 CD2 TYR A 311 74.254 −20.025 12.854 1.00 19.22 1502 CE1 TYR A 311 73.093 −19.612 10.395 1.00 21.56 1503 CE2 TYR A 311 75.018 −20.203 11.703 1.00 20.95 1504 CZ TYR A 311 74.425 −19.993 10.480 1.00 21.56 1505 OH TYR A 311 75.159 −20.170 9.329 1.00 24.43 1506 N ASP A 312 70.069 −21.385 16.314 1.00 22.16 1507 CA ASP A 312 69.147 −21.132 17.421 1.00 24.33 1508 C ASP A 312 69.426 −21.956 18.667 1.00 22.29 1509 O ASP A 312 69.166 −23.155 18.676 1.00 22.82 1510 CB ASP A 312 67.703 −21.360 16.940 1.00 25.85 1511 CG ASP A 312 66.717 −20.989 18.046 1.00 30.43 1512 OD1 ASP A 312 66.756 −19.889 18.609 1.00 30.37 1513 OD2 ASP A 312 65.841 −21.814 18.382 1.00 33.45 1514 N TYR A 313 69.905 −21.325 19.725 1.00 21.56 1515 CA TYR A 313 70.305 −22.052 20.933 1.00 21.31 1516 C TYR A 313 69.224 −21.924 21.996 1.00 22.83 1517 O TYR A 313 68.987 −20.799 22.457 1.00 20.91 1518 CB TYR A 313 71.644 −21.503 21.452 1.00 20.67 1519 CG TYR A 313 72.137 −22.255 22.674 1.00 19.10 1520 CD1 TYR A 313 72.697 −23.521 22.532 1.00 18.67 1521 CD2 TYR A 313 71.998 −21.744 23.956 1.00 18.42 1522 CE1 TYR A 313 73.148 −24.247 23.621 1.00 19.13 1523 CE2 TYR A 313 72.416 −22.475 25.069 1.00 17.61 1524 CZ TYR A 313 72.994 −23.703 24.889 1.00 19.22 1525 OH TYR A 313 73.413 −24.442 25.989 1.00 18.27 1526 N SER A 314 68.599 −23.055 22.329 1.00 23.06 1527 CA SER A 314 67.542 −23.000 23.332 1.00 25.19 1528 C SER A 314 67.926 −23.474 24.719 1.00 25.25 1529 O SER A 314 67.000 −23.528 25.550 1.00 25.31 1530 CB SER A 314 66.307 −23.804 22.843 1.00 27.03 1531 OG SER A 314 66.672 −25.175 22.739 1.00 28.18 1532 N GLY A 315 69.182 −23.694 25.070 1.00 24.12 1533 CA GLY A 315 69.527 −24.093 26.451 1.00 24.72 1534 C GLY A 315 69.338 −22.967 27.453 1.00 25.47 1535 O GLY A 315 69.165 −21.816 27.048 1.00 26.04 1536 N ASN A 316 69.339 −23.228 28.754 1.00 25.24 1537 CA ASN A 316 69.116 −22.249 29.805 1.00 25.73 1538 C ASN A 316 70.397 −21.804 30.509 1.00 25.95 1539 O ASN A 316 70.298 −21.278 31.638 1.00 24.29 1540 CB ASN A 316 68.190 −22.893 30.866 1.00 29.42 1541 CG ASN A 316 68.861 −23.980 31.705 1.00 33.78 1542 OD1 ASN A 316 70.048 −24.341 31.528 1.00 33.72 1543 ND2 ASN A 316 68.154 −24.553 32.687 1.00 34.41 1544 N ASP A 317 71.584 −22.038 29.911 1.00 21.74 1545 CA ASP A 317 72.807 −21.719 30.606 1.00 21.65 1546 C ASP A 317 73.650 −20.592 30.037 1.00 22.99 1547 O ASP A 317 74.868 −20.599 30.297 1.00 22.74 1548 CB ASP A 317 73.665 −23.009 30.705 1.00 22.71 1549 CG ASP A 317 74.073 −23.483 29.316 1.00 23.13 1550 OD1 ASP A 317 73.271 −23.346 28.363 1.00 22.02 1551 OD2 ASP A 317 75.185 −24.003 29.157 1.00 22.43 1552 N LEU A 318 73.097 −19.656 29.260 1.00 22.59 1553 CA LEU A 318 73.889 −18.531 28.754 1.00 20.66 1554 C LEU A 318 74.316 −17.676 29.955 1.00 20.42 1555 O LEU A 318 73.547 −17.564 30.903 1.00 17.61 1556 CB LEU A 318 73.169 −17.678 27.715 1.00 20.60 1557 CG LEU A 318 72.798 −18.391 26.385 1.00 19.68 1558 CD1 LEU A 318 71.963 −17.493 25.495 1.00 17.29 1559 CD2 LEU A 318 74.109 −18.776 25.680 1.00 16.96 1560 N GLY A 319 75.550 −17.187 29.890 1.00 20.73 1561 CA GLY A 319 76.193 −16.428 30.949 1.00 20.43 1562 C GLY A 319 77.202 −17.295 31.721 1.00 22.10 1563 O GLY A 319 77.914 −18.124 31.117 1.00 21.40 1564 N ASN A 320 77.286 −17.098 33.042 1.00 19.98 1565 CA ASN A 320 78.191 −17.952 33.835 1.00 21.91 1566 C ASN A 320 77.375 −18.729 34.867 1.00 22.53 1567 O ASN A 320 76.333 −18.231 35.331 1.00 21.27 1568 CB ASN A 320 79.297 −17.159 34.508 1.00 21.04 1569 CG ASN A 320 78.807 −16.191 35.571 1.00 21.43 1570 OD1 ASN A 320 78.574 −16.655 36.680 1.00 22.62 1571 ND2 ASN A 320 78.589 −14.900 35.304 1.00 18.58 1572 N VAL A 321 77.797 −19.940 35.176 1.00 22.76 1573 CA VAL A 321 77.084 −20.812 36.124 1.00 22.43 1574 C VAL A 321 78.113 −21.225 37.192 1.00 24.11 1575 O VAL A 321 78.998 −22.018 36.899 1.00 23.74 1576 CB VAL A 321 76.477 −22.041 35.464 1.00 24.06 1577 CG1 VAL A 321 75.861 −23.044 36.476 1.00 25.33 1578 CG2 VAL A 321 75.396 −21.628 34.452 1.00 23.25 1579 N TYR A 322 78.040 −20.600 38.364 1.00 24.47 1580 CA TYR A 322 79.021 −20.745 39.416 1.00 26.10 1581 C TYR A 322 78.764 −21.897 40.382 1.00 26.90 1582 O TYR A 322 77.658 −22.184 40.816 1.00 25.89 1583 CB TYR A 322 79.122 −19.432 40.251 1.00 25.11 1584 CG TYR A 322 79.911 −19.624 41.541 1.00 25.40 1585 CD1 TYR A 322 81.291 −19.576 41.519 1.00 25.69 1586 CD2 TYR A 322 79.282 −19.866 42.764 1.00 25.12 1587 CE1 TYR A 322 82.037 −19.772 42.669 1.00 26.68 1588 CE2 TYR A 322 80.010 −20.046 43.920 1.00 26.18 1589 CZ TYR A 322 81.383 −19.999 43.871 1.00 26.75 1590 OH TYR A 322 82.145 −20.197 44.987 1.00 27.96 1591 N SER A 323 79.858 −22.517 40.812 1.00 27.80 1592 CA SER A 323 79.884 −23.498 41.882 1.00 28.44 1593 C SER A 323 81.291 −23.469 42.494 1.00 28.56 1594 O SER A 323 82.252 −22.944 41.901 1.00 26.33 1595 CB SER A 323 79.467 −24.897 41.536 1.00 27.55 1596 OG SER A 323 80.342 −25.551 40.633 1.00 29.60 1597 N LYS A 324 81.399 −24.048 43.683 1.00 29.32 1598 CA LYS A 324 82.674 −24.064 44.394 1.00 31.61 1599 C LYS A 324 83.804 −24.679 43.609 1.00 30.15 1600 O LYS A 324 84.882 −24.101 43.574 1.00 29.36 1601 CB LYS A 324 82.529 −24.863 45.697 1.00 35.71 1602 CG LYS A 324 82.413 −23.989 46.937 1.00 40.11 1603 CD LYS A 324 82.177 −24.926 48.134 1.00 42.85 1604 CE LYS A 324 80.695 −25.015 48.452 1.00 44.71 1605 NZ LYS A 324 80.253 −23.993 49.436 1.00 46.25 1606 N ASP A 325 83.595 −25.836 42.979 1.00 30.61 1607 CA ASP A 325 84.674 −26.467 42.219 1.00 31.24 1608 C ASP A 325 84.934 −25.989 40.810 1.00 30.11 1609 O ASP A 325 86.033 −26.273 40.306 1.00 28.10 1610 CB ASP A 325 84.425 −27.990 42.162 1.00 34.10 1611 CG ASP A 325 84.438 −28.490 43.607 1.00 38.46 1612 OD1 ASP A 325 85.027 −27.884 44.523 1.00 39.44 1613 OD2 ASP A 325 83.746 −29.499 43.857 1.00 40.94 1614 N ALA A 326 84.007 −25.274 40.168 1.00 26.93 1615 CA ALA A 326 84.226 −24.816 38.800 1.00 24.07 1616 C ALA A 326 83.169 −23.821 38.324 1.00 23.18 1617 O ALA A 326 82.044 −23.822 38.845 1.00 23.26 1618 CB ALA A 326 84.066 −26.016 37.844 1.00 25.03 1619 N THR A 327 83.521 −23.011 37.326 1.00 22.27 1620 CA THR A 327 82.521 −22.114 36.751 1.00 22.23 1621 C THR A 327 82.410 −22.371 35.241 1.00 23.00 1622 O THR A 327 83.464 −22.441 34.587 1.00 22.16 1623 CB THR A 327 82.822 −20.630 36.971 1.00 22.19 1624 OG1 THR A 327 82.652 −20.444 38.359 1.00 20.51 1625 CG2 THR A 327 81.815 −19.716 36.226 1.00 21.57 1626 N SER A 328 81.189 −22.495 34.728 1.00 20.66 1627 CA SER A 328 81.065 −22.697 33.273 1.00 21.04 1628 C SER A 328 80.570 −21.437 32.555 1.00 21.82 1629 O SER A 328 79.704 −20.724 33.080 1.00 20.39 1630 CB SER A 328 80.013 −23.762 33.010 1.00 22.57 1631 OG SER A 328 80.420 −25.021 33.487 1.00 26.12 1632 N PHE A 329 81.055 −21.187 31.335 1.00 20.94 1633 CA PHE A 329 80.703 −19.990 30.587 1.00 19.32 1634 C PRE A 329 80.108 −20.361 29.232 1.00 20.62 1635 O PHE A 329 80.520 −21.374 28.618 1.00 18.58 1636 CB PHE A 329 81.937 −19.097 30.414 1.00 17.82 1637 CG PHE A 329 82.637 −18.648 31.677 1.00 19.59 1638 CD1 PHE A 329 83.556 −19.478 32.308 1.00 16.87 1639 CD2 PHE A 329 82.377 −17.385 32.209 1.00 19.26 1640 CE1 PHE A 329 84.195 −19.074 33.465 1.00 19.15 1641 CE2 PHE A 329 83.064 −16.954 33.344 1.00 18.66 1642 CZ PHE A 329 83.904 −17.819 33.995 1.00 19.30 1643 N ARG A 330 79.142 −19.576 28.754 1.00 19.04 1644 CA ARG A 330 78.571 −19.791 27.432 1.00 17.97 1645 C ARG A 330 78.029 −18.474 26.858 1.00 19.63 1646 O ARG A 330 77.319 −17.717 27.557 1.00 18.47 1647 CB ARG A 330 77.471 −20.860 27.393 1.00 20.74 1648 CG ARG A 330 77.092 −21.262 25.948 1.00 21.20 1649 CD ARG A 330 75.983 −22.295 25.893 1.00 21.96 1650 NE ARG A 330 76.296 −23.594 26.492 1.00 22.92 1651 CZ ARG A 330 76.812 −24.638 25.839 1.00 23.47 1652 NH1 ARG A 330 77.076 −25.760 26.503 1.00 23.14 1653 NH2 ARG A 330 77.034 −24.625 24.528 1.00 20.70 1654 N VAL A 331 78.421 −18.196 25.605 1.00 18.50 1655 CA VAL A 331 77.991 −16.939 24.952 1.00 18.28 1656 C VAL A 331 77.605 −17.227 23.505 1.00 17.84 1657 O VAL A 331 78.271 −18.081 22.888 1.00 17.02 1658 CB VAL A 331 79.103 −15.885 25.030 1.00 17.74 1659 CG1 VAL A 331 80.369 −16.391 24.320 1.00 18.41 1660 CG2 VAL A 331 78.693 −14.550 24.422 1.00 18.27 1661 N TRP A 332 76.561 −15.576 22.985 1.00 17.30 1662 CA TRP A 332 76.128 −16.832 21.606 1.00 16.55 1663 C TRP A 332 76.872 −15.925 20.635 1.00 16.29 1664 O TRP A 332 76.694 −14.711 20.747 1.00 16.81 1665 CB TRP A 332 74.607 −16.801 21.475 1.00 15.95 1666 CG TRP A 332 73.976 −17.064 20.126 1.00 16.61 1667 CD1 TRP A 332 73.873 −18.291 19.532 1.00 16.92 1668 CD2 TRP A 332 73.332 −16.134 19.237 1.00 16.47 1669 NE1 TRP A 332 73.231 −18.170 18.311 1.00 18.27 1670 CE2 TRP A 332 72.866 −16.865 18.119 1.00 17.73 1671 CE3 TRP A 332 73.178 −14.747 19.217 1.00 16.21 1672 CZ2 TRP A 332 72.274 −16.256 17.010 1.00 16.41 1673 CZ3 TRP A 332 72.531 −14.138 18.143 1.00 16.52 1674 CH2 TRP A 332 72.075 −14.905 17.057 1.00 15.60 1675 N ALA A 333 77.714 −16.446 19.737 1.00 16.60 1676 CA ALA A 333 78.444 −15.553 18.786 1.00 17.43 1677 C ALA A 333 78.657 −16.275 17.466 1.00 17.33 1678 O ALA A 333 79.767 −16.726 17.165 1.00 17.44 1679 CB ALA A 333 79.803 −15.187 19.395 1.00 17.32 1680 N PRO A 334 77.615 −16.422 16.640 1.00 16.81 1681 CA PRO A 334 77.667 −17.222 15.426 1.00 16.90 1682 C PRO A 334 78.499 −16.717 14.264 1.00 18.01 1683 O PRO A 334 78.812 −17.501 13.340 1.00 19.09 1684 CB PRO A 334 76.165 −17.379 15.095 1.00 17.28 1685 CG PRO A 334 75.567 −16.049 15.533 1.00 17.13 1686 CD PRO A 334 76.259 −15.842 16.881 1.00 15.63 1687 N THR A 335 78.966 −15.478 14.258 1.00 17.49 1688 CA THR A 335 79.765 −14.969 13.145 1.00 19.36 1689 C THR A 335 81.245 −14.804 13.484 1.00 19.67 1690 O THR A 335 82.095 −14.363 12.681 1.00 19.24 1691 CB THR A 335 79.202 −13.632 12.595 1.00 19.04 1692 OG1 THR A 335 79.459 −12.557 13.518 1.00 18.31 1693 CG2 THR A 335 77.709 −13.744 12.268 1.00 18.55 1694 N ALA A 336 81.589 −15.082 14.737 1.00 20.15 1695 CA ALA A 336 82.961 −14.943 15.225 1.00 21.16 1696 C ALA A 336 83.915 −16.034 14.731 1.00 20.66 1697 O ALA A 336 83.522 −17.199 14.668 1.00 20.80 1698 CB ALA A 336 82.965 −15.048 16.765 1.00 19.61 1699 N SER A 337 85.164 −15.642 14.454 1.00 21.24 1700 CA SER A 337 86.158 −16.646 14.033 1.00 21.72 1701 C SER A 337 86.913 −17.153 15.263 1.00 22.44 1702 O SER A 337 87.457 −18.262 15.262 1.00 22.33 1703 CB SER A 337 87.101 −16.133 12.942 1.00 19.79 1704 OG SER A 337 87.842 −15.014 13.378 1.00 19.73 1705 N ASN A 338 86.800 −16.461 16.395 1.00 22.39 1706 CA ASN A 338 87.474 −16.897 17.629 1.00 22.59 1707 C ASN A 338 86.895 −16.133 18.822 1.00 21.70 1708 O ASN A 338 86.551 −14.961 18.862 1.00 20.21 1709 CB ASN A 338 88.985 −16.546 17.593 1.00 23.25 1710 CG ASN A 338 89.769 −17.286 18.665 1.00 23.27 1711 OD1 ASN A 338 89.309 −18.312 19.176 1.00 24.41 1712 ND2 ASN A 338 90.949 −18.819 19.009 1.00 22.31 1713 N VAL A 339 86.788 −16.750 19.982 1.00 20.64 1714 CA VAL A 339 86.296 −16.110 21.195 1.00 20.83 1715 C VAL A 339 87.216 −16.633 22.325 1.00 21.76 1716 O VAL A 339 87.446 −17.852 22.405 1.00 20.76 1717 CB VAL A 339 84.849 −16.455 21.599 1.00 20.75 1718 CG1 VAL A 339 84.446 −15.701 22.879 1.00 20.39 1719 CG2 VAL A 339 83.840 −16.157 20.492 1.00 20.29 1720 N GLN A 340 87.759 −15.716 23.111 1.00 19.11 1721 CA GLN A 340 88.577 −16.086 24.253 1.00 21.95 1722 C GLN A 340 87.972 −15.504 25.543 1.00 22.76 1723 O GLN A 340 87.332 −14.438 25.536 1.00 20.68 1724 CB GLN A 340 90.005 −15.531 24.024 1.00 25.09 1725 CG GLN A 340 90.662 −16.091 22.738 1.00 28.48 1726 CD GLN A 340 92.158 −15.840 22.679 1.00 32.41 1727 OE1 GLN A 340 92.611 −14.980 21.913 1.00 34.76 1728 NE2 GLN A 340 92.927 −16.566 23.479 1.00 32.06 1729 N LEU A 341 88.203 −16.164 26.673 1.00 21.03 1730 CA LEU A 341 87.802 −15.701 27.996 1.00 19.98 1731 C LEU A 341 88.980 −14.997 28.691 1.00 20.18 1732 O LEU A 341 90.067 −15.556 28.788 1.00 18.71 1733 CB LEU A 341 87.383 −16.917 28.829 1.00 19.90 1734 CG LEU A 341 86.998 −16.678 30.295 1.00 21.43 1735 CD1 LEU A 341 85.703 −15.837 30.345 1.00 20.84 1736 CD2 LEU A 341 86.828 −18.018 31.006 1.00 20.08 1737 N LEU A 342 88.796 −13.750 29.074 1.00 19.42 1738 CA LEU A 342 89.731 −12.963 29.842 1.00 21.69 1739 C LEU A 342 89.252 −12.963 31.306 1.00 22.85 1740 O LEU A 342 88.125 −12.555 31.541 1.00 21.27 1741 CB LEU A 342 89.901 −11.557 29.277 1.00 22.45 1742 CG LEU A 342 90.120 −11.437 27.750 1.00 23.01 1743 CD1 LEU A 342 90.324 −9.977 27.354 1.00 20.48 1744 CD2 LEU A 342 91.270 −12.283 27.239 1.00 24.22 1745 N LEU A 343 90.090 −13.551 32.167 1.00 21.42 1746 CA LEU A 343 89.834 −13.675 33.594 1.00 22.82 1747 C LEU A 343 90.771 −12.755 34.359 1.00 23.56 1748 O LEU A 343 91.973 −12.618 34.049 1.00 22.34 1749 CB LEU A 343 89.977 −15.095 34.112 1.00 23.13 1750 CG LEU A 343 88.936 −16.134 33.765 1.00 24.04 1751 CD1 LEU A 343 89.386 −17.523 34.242 1.00 22.59 1752 CD2 LEU A 343 87.574 −15.819 34.402 1.00 22.28 1753 N TYR A 344 90.187 −12.001 3.296 1.00 21.67 1754 CA TYR A 344 90.891 −11.029 36.081 1.00 20.84 1755 C TYR A 344 90.731 −11.309 37.578 1.00 22.98 1756 O TYR A 344 89.95 −11.488 38.042 1.00 20.73 1757 CB TYR A 344 90.471 −9.590 35.781 1.00 22.01 1758 CG TYR A 344 90.514 −9.119 34.350 1.00 22.91 1759 CD1 TYR A 344 89.464 −9.443 33.473 1.00 23.47 1760 CD2 TYR A 344 91.589 −8.413 33.839 1.00 23.31 1761 CE1 TYR A 344 89.503 −9.068 32.134 1.00 22.88 1762 CE2 TYR A 344 91.600 −7.977 32.516 1.00 24.05 1763 CZ TYR A 344 90.574 −8.343 31.665 1.00 23.45 1764 OH TYR A 344 90.607 −7.928 30.344 1.00 21.39 1765 N ASN A 345 91.843 −11.311 38.344 1.00 23.99 1766 CA ASN A 345 91.708 −11.557 39.793 1.00 26.27 1767 C ASN A 345 91.603 −10.255 40.558 1.00 26.36 1768 O ASN A 345 91.850 −10.193 41.752 1.00 28.06 1769 CB ASN A 345 92.841 −12.427 40.366 1.00 27.33 1770 CG ASN A 345 94.204 −11.783 40.253 1.00 27.96 1771 OD1 ASN A 345 94.333 −10.580 39.995 1.00 26.96 1772 ND2 ASN A 345 95.254 −12.588 40.461 1.00 30.19 1773 N SER A 346 91.183 −9.172 39.904 1.00 27.11 1774 CA SER A 346 91.040 −7.885 40.569 1.00 26.45 1775 C SER A 346 90.101 −7.018 39.745 1.00 26.06 1776 O SER A 346 89.895 −7.299 38.564 1.00 26.29 1777 CB SER A 346 92.413 −7.241 40.740 1.00 24.63 1778 OG SER A 346 92.769 −6.551 39.569 1.00 23.97 1779 N GLU A 347 89.587 −5.953 40.320 1.00 25.01 1780 CA GLU A 347 88.629 −5.103 39.610 1.00 26.48 1781 C GLU A 347 89.285 −4.207 38.593 1.00 27.56 1782 O GLU A 347 88.618 −3.846 37.608 1.00 26.07 1783 CB GLU A 347 87.833 −4.290 40.665 1.00 26.52 1784 CG GLU A 347 86.563 −3.647 40.158 1.00 25.42 1785 CD GLU A 347 85.681 −3.082 41.265 1.00 25.59 1786 OE1 GLU A 347 84.477 −2.829 41.018 1.00 23.17 1787 OE2 GLU A 347 86.140 −2.884 42.416 1.00 24.63 1788 N LYS A 348 90.532 −3.758 38.843 1.00 27.94 1789 CA LYS A 348 91.239 −2.907 37.892 1.00 30.23 1790 C LYS A 348 92.602 −3.443 37.434 1.00 30.18 1791 O LYS A 348 93.183 −2.871 36.515 1.00 30.31 1792 CB LYS A 348 91.496 −1.484 38.403 1.00 32.74 1793 CG LYS A 348 90.350 −0.740 39.058 1.00 36.60 1794 CD LYS A 348 90.397 −0.890 40.579 1.00 39.69 1795 CE LYS A 348 91.755 −0.453 41.157 1.00 40.78 1796 NZ LYS A 348 91.956 −0.820 42.572 1.00 40.05 1797 N GLY A 349 93.121 −4.508 38.002 1.00 29.40 1798 CA GLY A 349 94.413 −5.069 37.659 1.00 30.15 1799 C GLY A 349 94.469 −5.699 36.268 1.00 29.96 1800 O GLY A 349 93.436 −5.955 35.630 1.00 26.44 1801 N SER A 350 95.695 −5.979 35.812 1.00 27.06 1802 CA SER A 350 95.884 −6.505 34.472 1.00 26.80 1803 C SER A 350 95.470 −7.962 34.377 1.00 27.11 1804 O SER A 350 95.237 −8.656 35.366 1.00 26.51 1805 CB SER A 350 97.333 −6.250 33.997 1.00 28.64 1806 OG SER A 350 98.234 −7.164 34.581 1.00 25.07 1807 N ILE A 351 95.238 −8.418 33.148 1.00 27.83 1808 CA ILE A 351 94.751 −9.754 32.873 1.00 27.61 1809 C ILE A 351 95.544 −10.819 33.604 1.00 28.09 1810 O ILE A 351 96.782 −10.849 33.632 1.00 25.86 1811 CB ILE A 351 94.698 −10.042 31.362 1.00 30.70 1812 CG1 ILE A 351 94.270 −11.501 31.097 1.00 30.30 1813 CG2 ILE A 351 96.082 −9.848 30.749 1.00 32.44 1814 CD1 ILE A 351 93.598 −11.582 29.747 1.00 33.45 1815 N THR A 352 94.804 −11.747 34.211 1.00 26.74 1816 CA THR A 352 95.382 −12.823 34.980 1.00 27.48 1817 C THR A 352 95.555 −14.073 34.136 1.00 28.86 1818 O THR A 352 96.539 −14.780 34.332 1.00 29.06 1819 CB THR A 352 94.507 −13.196 36.212 1.00 26.13 1820 OG1 THR A 352 94.336 −11.981 36.927 1.00 25.38 1821 CG2 THR A 352 95.178 −14.198 37.140 1.00 27.23 1822 N LYS A 353 94.575 −14.379 33.308 1.00 28.99 1823 CA LYS A 353 94.536 −15.603 32.517 1.00 31.07 1824 C LYS A 353 93.738 −15.337 31.224 1.00 31.82 1825 O LYS A 353 92.623 −14.771 31.223 1.00 26.80 1826 CB LYS A 353 93.848 −16.644 33.383 1.00 34.73 1827 CG LYS A 353 94.468 −17.997 33.598 1.00 40.91 1828 CD LYS A 353 93.462 −19.025 34.085 1.00 44.90 1829 CE LYS A 353 93.470 −19.297 35.585 1.00 47.03 1830 NE LYS A 353 92.210 −20.014 35.986 1.00 47.57 1831 N GLN A 354 94.323 −15.729 30.091 1.00 29.04 1832 CA GLN A 354 93.676 −15.609 28.795 1.00 29.05 1833 C GLN A 354 93.487 −17.017 28.238 1.00 30.10 1834 O GLN A 354 94.488 −17.758 28.103 1.00 31.21 1835 CB GLN A 354 94.467 −14.688 27.880 1.00 29.18 1836 CG GLN A 354 93.905 −14.566 26.477 1.00 31.51 1837 CD GLN A 354 94.412 −13.380 25.699 1.00 35.08 1838 OE1 GLN A 354 94.375 −13.338 24.466 1.00 37.15 1839 NE2 GLN A 354 94.905 −12.320 26.329 1.00 37.06 1840 N LEU A 355 92.253 −17.454 28.014 1.00 25.86 1841 CA LEU A 355 91.935 −18.815 27.630 1.00 25.52 1842 C LEU A 355 91.099 −18.933 26.358 1.00 25.60 1843 O LEU A 355 90.052 −18.276 26.296 1.00 23.63 1844 CB LEU A 355 91.104 −19.459 28.763 1.00 23.98 1845 CG LEU A 355 91.678 −20.180 29.957 1.00 27.14 1846 CD1 LEU A 355 93.202 −20.110 30.090 1.00 24.35 1847 CD2 LEU A 355 91.046 −19.801 31.294 1.00 24.19 1848 N GLU A 356 91.388 −19.914 25.498 1.00 24.90 1849 CA GLU A 356 90.561 −20.149 24.328 1.00 25.07 1850 C GLU A 356 89.240 −20.795 24.749 1.00 24.27 1851 O GLU A 356 89.220 −21.728 25.556 1.00 24.57 1852 CB GLU A 356 91.263 −21.110 23.354 1.00 26.34 1853 CG GLU A 356 92.307 −20.425 22.486 1.00 28.70 1854 CD GLU A 356 91.664 −19.583 21.391 1.00 29.91 1855 OE1 GLU A 356 90.508 −19.768 20.973 1.00 30.84 1856 OE2 GLU A 356 92.360 −18.651 20.957 1.00 31.88 1857 N MET A 357 88.138 −20.398 24.144 1.00 24.03 1858 CA MET A 357 86.839 −21.025 24.390 1.00 21.73 1859 C MET A 357 86.645 −22.023 23.268 1.00 22.56 1860 O MET A 357 87.422 −21.932 22.306 1.00 23.10 1861 CB MET A 357 85.724 −19.974 24.468 1.00 20.62 1862 CG MET A 357 85.893 −19.016 25.636 1.00 19.78 1863 SD MET A 357 84.518 −17.881 25.954 1.00 18.56 1864 CE MET A 357 83.209 −19.002 26.424 1.00 17.50 1865 N GLN A 358 85.749 −22.969 23.351 1.00 23.45 1866 CA GLN A 358 85.504 −23.939 22.312 1.00 26.55 1867 C GLN A 358 84.150 −23.684 21.603 1.00 25.08 1868 O GLN A 358 83.110 −23.528 22.253 1.00 21.83 1869 CB GLN A 358 85.324 −25.373 22.847 1.00 29.06 1870 CG GLN A 358 85.931 −25.673 24.194 1.00 36.05 1871 CD GLN A 358 85.318 −26.928 24.804 1.00 38.87 1872 OE1 GLN A 358 85.386 −27.019 26.035 1.00 42.36 1873 NE2 GLN A 358 84.727 −27.807 23.987 1.00 40.44 1874 N LYS A 359 84.197 −23.798 20.304 1.00 24.04 1875 CA LYS A 359 83.007 −23.709 19.465 1.00 26.25 1876 C LYS A 359 82.043 −24.816 19.852 1.00 24.84 1877 O LYS A 359 82.493 −25.956 19.974 1.00 26.59 1878 CB LYS A 359 83.343 −23.834 17.978 1.00 26.51 1879 CG LYS A 359 82.110 −23.602 17.112 1.00 29.91 1880 CD LYS A 359 81.361 −22.329 17.504 1.00 30.23 1881 CE LYS A 359 79.954 −22.267 16.933 1.00 28.64 1882 NZ LYS A 359 80.031 −22.364 15.441 1.00 28.49 1883 N SER A 360 80.782 −24.516 20.104 1.00 23.90 1884 CA SER A 360 79.794 −25.489 20.549 1.00 23.71 1885 C SER A 360 78.515 −25.385 19.738 1.00 24.86 1886 O SER A 360 78.513 −24.861 18.608 1.00 23.35 1887 CB SER A 360 79.587 −25.315 22.070 1.00 23.14 1888 OG SER A 360 78.641 −26.216 22.656 1.00 22.35 1889 N ASP A 361 77.405 −25.945 20.249 1.00 23.82 1890 CA ASP A 361 76.173 −25.979 19.475 1.00 25.63 1891 C ASP A 361 75.582 −24.625 19.066 1.00 23.92 1892 O ASP A 361 75.515 −23.693 19.861 1.00 21.92 1893 CB ASP A 361 75.057 −26.676 20.281 1.00 29.13 1894 CG ASP A 361 75.440 −28.089 20.700 1.00 33.65 1895 OD1 ASP A 361 76.245 −28.789 20.062 1.00 34.34 1896 OD2 ASP A 361 74.868 −28.505 21.735 1.00 37.02 1897 N ASN A 362 74.897 −24.624 17.935 1.00 22.19 1898 CA ASN A 362 74.108 −23.504 17.439 1.00 20.84 1899 C ASN A 362 74.723 −22.135 17.566 1.00 20.78 1900 O ASN A 362 74.034 −21.188 18.003 1.00 22.45 1901 CB ASN A 362 72.734 −23.521 18.149 1.00 21.03 1902 CG ASN A 362 72.027 −24.871 18.007 1.00 21.03 1903 OD1 ASN A 362 71.503 −25.284 16.951 1.00 20.90 1904 ND2 ASN A 362 71.904 −25.578 19.095 1.00 17.27 1905 N GLY A 363 75.986 −21.960 17.142 1.00 19.74 1906 CA GLY A 363 76.621 −20.650 17.206 1.00 18.96 1907 C GLY A 363 77.260 −20.272 18.543 1.00 18.21 1908 O GLY A 363 77.931 −19.229 18.591 1.00 15.89 1909 N THR A 364 77.156 −21.080 19.578 1.00 15.00 1910 CA THR A 364 77.689 −20.699 20.880 1.00 17.37 1911 C THR A 364 79.156 −21.147 21.019 1.00 17.64 1912 O THR A 364 79.666 −21.891 20.195 1.00 17.37 1913 CB THR A 364 76.957 −21.274 22.108 1.00 17.36 1914 OG1 THR A 364 76.996 −22.715 22.132 1.00 18.13 1915 CG2 THR A 364 75.462 −20.902 22.195 1.00 18.48 1916 N TRP A 365 79.861 −20.549 21.955 1.00 17.83 1917 CA TRP A 365 81.196 −20.835 22.405 1.00 20.62 1918 C TRP A 365 81.074 −21.135 23.903 1.00 22.44 1919 O TRP A 365 80.263 −20.458 24.568 1.00 22.38 1920 CB TRP A 365 82.167 −19.660 22.183 1.00 19.73 1921 CG TRP A 365 82.409 −19.420 20.718 1.00 20.76 1922 CD1 TRP A 365 81.510 −18.888 19.822 1.00 19.99 1923 CD2 TRP A 365 83.597 −19.712 19.980 1.00 20.44 1924 NE1 TRP A 365 82.068 −18.850 18.572 1.00 20.24 1925 CE2 TRP A 365 83.351 −19.360 18.646 1.00 21.78 1926 CE3 TRP A 365 84.852 −20.236 20.320 1.00 22.22 1927 CZ2 TRP A 365 84.325 −19.484 17.645 1.00 21.66 1928 CZ3 TRP A 365 85.821 −20.393 19.335 1.00 22.86 1929 CH2 TRP A 365 85.540 −20.011 18.007 1.00 23.02 1930 N LYS A 366 81.789 −22.120 24.428 1.00 22.80 1931 CA LYS A 366 81.671 −22.479 25.839 1.00 23.01 1932 C LYS A 366 83.034 −22.735 26.462 1.00 24.27 1933 O LYS A 366 84.052 −22.851 25.763 1.00 22.69 1934 CB LYS A 366 80.802 −23.755 25.943 1.00 23.05 1935 CG LYS A 366 81.567 −25.016 25.499 1.00 23.62 1936 CD LYS A 366 80.702 −26.253 25.725 1.00 25.72 1937 CE LYS A 366 81.449 −27.535 25.340 1.00 28.42 1938 NZ LYS A 366 80.483 −28.675 25.518 1.00 30.63 1939 N LEU A 367 83.102 −22.838 27.785 1.00 24.03 1940 CA LEU A 367 84.359 −23.148 28.478 1.00 23.96 1941 C LEU A 367 84.084 −23.398 29.967 1.00 25.05 1942 O LEU A 367 83.301 −22.711 30.631 1.00 20.92 1943 CB LEU A 367 85.480 −22.129 28.320 1.00 24.83 1944 CG LEU A 367 86.823 −22.510 28.968 1.00 24.39 1945 CD1 LEU A 367 87.419 −23.727 28.264 1.00 24.41 1946 CD2 LEU A 367 87.859 −21.399 28.947 1.00 22.93 1947 N GLN A 368 84.576 −24.553 30.440 1.00 26.14 1948 CA GLN A 368 84.447 −24.893 31.849 1.00 27.03 1949 C GLN A 368 85.791 −24.611 32.529 1.00 26.26 1950 O GLN A 368 86.816 −25.102 32.007 1.00 23.19 1951 CB GLN A 368 84.045 −26.354 32.059 1.00 29.88 1952 CG GLN A 368 83.942 −26.621 33.557 1.00 34.12 1953 CD GLN A 368 83.326 −27.947 33.888 1.00 38.21 1954 OE1 GLN A 368 82.163 −28.268 33.661 1.00 41.75 1955 NE2 GLN A 368 84.076 −28.846 34.488 1.00 39.92 1956 N VAL A 369 85.811 −23.779 33.570 1.00 25.22 1957 CA VAL A 369 87.072 −23.466 34.227 1.00 26.94 1958 C VAL A 369 87.104 −24.075 35.641 1.00 27.56 1959 O VAL A 369 86.251 −23.711 36.453 1.00 26.74 1960 CB VAL A 369 87.404 −21.975 34.403 1.00 27.02 1961 CG1 VAL A 369 88.793 −21.803 35.043 1.00 28.37 1962 CG2 VAL A 369 87.375 −21.200 33.086 1.00 26.62 1963 N SER A 370 88.133 −24.863 35.929 1.00 27.55 1964 CA SER A 370 88.332 −25.436 37.261 1.00 30.11 1965 C SER A 370 88.809 −24.485 38.333 1.00 27.75 1966 O SER A 370 89.579 −23.573 38.078 1.00 28.00 1967 CB SER A 370 89.397 −26.574 37.177 1.00 31.50 1968 OG SER A 370 88.799 −27.545 36.318 1.00 35.78 1969 N GLY A 371 88.380 −24.676 39.577 1.00 31.30 1970 CA GLY A 371 88.784 −23.771 40.670 1.00 30.93 1971 C GLY A 371 87.571 −22.927 41.091 1.00 32.19 1972 O GLY A 371 86.518 −22.988 40.453 1.00 30.29 1973 N ASN A 372 87.725 −22.211 42.194 1.00 31.23 1974 CA ASN A 372 86.626 −21.395 42.752 1.00 31.68 1975 C ASN A 372 86.774 −19.969 42.243 1.00 28.25 1976 O ASN A 372 87.724 −19.265 42.643 1.00 28.03 1977 CB ASN A 372 86.716 −21.406 44.286 1.00 33.96 1978 CG ASN A 372 85.534 −20.773 44.992 1.00 36.29 1979 OD1 ASN A 372 84.864 −19.865 44.493 1.00 35.90 1980 ND2 ASN A 372 85.211 −21.241 46.212 1.00 35.53 1981 N LEU A 373 85.865 −19.526 41.377 1.00 25.26 1982 CA LEU A 373 86.006 −18.204 40.775 1.00 23.40 1983 C LEU A 373 85.148 −17.151 41.456 1.00 22.75 1984 O LEU A 373 84.924 −16.071 40.902 1.00 20.78 1985 CB LEU A 373 85.754 −18.243 39.260 1.00 23.70 1986 CG LEU A 373 86.733 −19.077 38.413 1.00 24.26 1987 CD1 LEU A 373 86.538 −18.827 36.918 1.00 24.86 1988 CD2 LEU A 373 88.185 −18.745 38.729 1.00 26.18 1989 N GLU A 374 84.705 −17.422 42.691 1.00 22.76 1990 CA GLU A 374 83.955 −16.376 43.386 1.00 20.88 1991 C GLU A 374 84.658 −15.013 43.353 1.00 21.01 1992 O GLU A 374 85.868 −14.894 43.493 1.00 18.90 1993 CB GLU A 374 83.722 −16.806 44.835 1.00 23.51 1994 CG GLU A 374 82.766 −15.862 45.565 1.00 25.57 1995 CD GLU A 374 82.144 −16.577 46.741 1.00 29.28 1996 OE1 GLU A 374 82.604 −17.657 47.084 1.00 29.30 1997 OE2 GLU A 374 81.193 −16.042 47.307 1.00 27.72 1998 N ASN A 375 83.841 −13.965 43.118 1.00 19.21 1999 CA ASN A 375 84.357 −12.596 43.101 1.00 19.30 2000 C ASN A 375 85.512 −12.400 42.116 1.00 19.99 2001 O ASN A 375 86.381 −11.553 42.288 1.00 18.96 2002 CB ASN A 375 84.810 −12.224 44.515 1.00 21.23 2003 CG ASN A 375 83.658 −12.390 45.469 1.00 22.98 2004 OD1 ASN A 375 83.828 −12.711 46.642 1.00 21.72 2005 ND2 ASN A 375 82.446 −12.157 44.937 1.00 19.08 2006 N TRP A 376 85.534 −13.250 41.077 1.00 18.63 2007 CA TRP A 376 86.479 −13.023 39.991 1.00 20.31 2008 C TRP A 376 85.998 −12.050 38.948 1.00 20.90 2009 O TRP A 376 84.705 −11.885 38.809 1.00 20.95 2010 CB TRP A 376 86.796 −14.374 39.348 1.00 21.71 2011 CG TRP A 376 87.964 −15.000 40.012 1.00 22.49 2012 CD1 TRP A 376 88.036 −15.457 41.347 1.00 20.13 2013 CD2 TRP A 376 89.290 −15.156 39.450 1.00 22.92 2014 NE1 TRP A 376 89.280 −15.887 41.683 1.00 20.87 2015 CE2 TRP A 376 90.116 −15.690 40.471 1.00 22.98 2016 CE3 TRP A 376 89.839 −14.871 38.203 1.00 23.59 2017 CZ2 TRP A 376 91.464 −15.903 40.230 1.00 23.06 2018 CZ3 TRP A 376 91.187 −15.088 37.962 1.00 24.45 2019 CH2 TRP A 376 92.005 −15.606 38.983 1.00 23.52 2020 N TYR A 377 86.618 −11.303 38.111 1.00 19.49 2021 CA TYR A 377 86.016 −10.505 37.051 1.00 19.50 2022 C TYR A 377 86.358 −11.145 35.703 1.00 20.68 2023 O TYR A 377 87.330 −11.914 35.605 1.00 19.41 2024 CB TYR A 377 86.409 −9.027 37.144 1.00 17.91 2025 CG TYR A 377 85.956 −8.348 38.427 1.00 18.83 2026 CD1 TYR A 377 86.708 −8.461 39.604 1.00 19.72 2027 CD2 TYR A 377 84.808 −7.586 38.514 1.00 17.93 2028 CE1 TYR A 377 86.334 −7.877 40.796 1.00 18.37 2029 CE2 TYR A 377 84.394 −6.978 39.692 1.00 17.34 2030 CZ TYR A 377 85.181 −7.130 40.849 1.00 20.22 2031 OH TYR A 377 84.783 −6.517 42.039 1.00 15.40 2032 N TYR A 378 85.628 −10.823 34.626 1.00 20.04 2033 CA TYR A 378 85.785 −11.425 33.337 1.00 19.08 2034 C TYR A 378 85.235 −10.613 32.166 1.00 19.99 2035 O TYR A 378 84.354 −9.760 32.334 1.00 20.17 2036 CB TYR A 378 85.171 −12.819 33.281 1.00 18.87 2037 CG TYR A 378 83.675 −13.049 33.109 1.00 19.44 2038 CD1 TYR A 378 83.148 −13.529 31.906 1.00 17.38 2039 CD2 TYR A 378 82.794 −12.845 34.175 1.00 17.88 2040 CE1 TYR A 378 81.784 −13.770 31.768 1.00 18.82 2041 CE2 TYR A 378 81.431 −13.071 34.036 1.00 18.35 2042 CZ TYR A 378 80.926 −13.553 32.837 1.00 17.91 2043 OH TYR A 378 79.558 −13.797 32.732 1.00 18.43 2044 N LEU A 379 85.839 −10.897 30.993 1.00 17.82 2045 CA LEU A 379 85.409 −10.274 29.738 1.00 17.08 2046 C LEU A 379 85.510 −11.341 28.635 1.00 18.66 2047 O LEU A 379 86.145 −12.370 28.873 1.00 15.93 2048 CB LEU A 379 86.246 −9.088 29.300 1.00 17.38 2049 CG LEU A 379 86.193 −7.747 30.010 1.00 19.69 2050 CD1 LEU A 379 87.317 −6.812 29.589 1.00 16.36 2051 CD2 LEU A 379 84.837 −7.062 29.750 1.00 18.77 2052 N TYR A 380 84.730 −11.180 27.547 1.00 19.37 2053 CA TYR A 380 84.862 −12.039 26.387 1.00 19.03 2054 C TYR A 380 85.691 −11.243 25.346 1.00 19.03 2055 O TYR A 380 85.468 −10.031 25.169 1.00 20.13 2056 CB TYR A 380 83.558 −12.495 25.715 1.00 17.35 2057 CG TYR A 380 82.665 −13.391 26.562 1.00 17.93 2058 CD1 TYR A 380 81.332 −13.060 26.782 1.00 17.57 2059 CD2 TYR A 380 83.146 −14.541 27.170 1.00 16.75 2060 CE1 TYR A 380 80.485 −13.866 27.548 1.00 18.52 2061 CE2 TYR A 380 82.344 −15.343 27.948 1.00 17.90 2062 CZ TYR A 380 81.011 −15.013 28.134 1.00 17.98 2063 OH TYR A 380 80.229 −15.823 28.913 1.00 16.91 2064 N GLN A 381 86.621 −11.910 24.682 1.00 18.61 2065 CA GLN A 381 87.401 −11.198 23.645 1.00 19.39 2066 C GLN A 381 86.998 −11.824 22.307 1.00 17.85 2067 O GLN A 381 87.207 −13.010 22.046 1.00 17.98 2068 CB GLN A 381 88.897 −11.285 23.867 1.00 19.69 2069 CG GLN A 381 89.727 −10.637 22.755 1.00 22.60 2070 CD GLN A 381 91.215 −10.720 23.077 1.00 26.02 2071 OE1 GLN A 381 91.901 −11.578 22.528 1.00 29.96 2072 NE2 GLN A 381 91.773 −9.888 23.933 1.00 24.48 2073 N VAL A 382 86.238 −11.084 21.522 1.00 16.71 2074 CA VAL A 382 85.570 −11.634 20.346 1.00 16.94 2075 C VAL A 382 86.212 −11.103 19.051 1.00 17.81 2076 O VAL A 382 86.315 −9.892 18.865 1.00 17.01 2077 CB VAL A 382 84.070 −11.250 20.358 1.00 17.30 2078 CG1 VAL A 382 83.329 −11.902 19.195 1.00 15.09 2079 CG2 VAL A 382 83.383 −11.617 21.704 1.00 15.18 2080 N THR A 383 86.582 −12.029 18.170 1.00 17.62 2081 CA THR A 383 87.183 −11.717 16.889 1.00 18.58 2082 C THR A 383 86.147 −11.913 15.773 1.00 20.31 2083 O THR A 383 85.654 −13.000 15.528 1.00 20.06 2084 CB THR A 383 88.445 −12.526 16.483 1.00 15.89 2085 OG1 THR A 383 89.447 −12.219 17.481 1.00 16.62 2086 CG2 THR A 383 89.035 −12.075 15.135 1.00 16.58 2087 N VAL A 384 85.721 −10.804 15.246 1.00 22.99 2088 CA VAL A 384 84.757 −10.704 14.157 1.00 29.90 2089 C VAL A 384 85.220 −10.119 12.820 1.00 33.88 2090 O VAL A 384 85.356 −8.914 12.654 1.00 35.70 2091 CB VAL A 384 83.363 −10.325 14.691 1.00 30.03 2092 CG1 VAL A 384 82.464 −10.504 13.470 1.00 29.72 2093 CG2 VAL A 384 82.691 −10.944 15.902 1.00 28.84 2094 N ASN A 385 85.449 −11.060 11.887 1.00 20.00 2095 CA ASN A 385 85.893 −10.615 10.580 1.00 20.00 2096 C ASN A 385 87.128 −9.723 10.723 1.00 20.00 2097 O ASN A 385 87.146 −8.572 10.307 1.00 20.00 2098 CB ASN A 385 84.918 −10.260 9.442 1.00 20.00 2099 CG ASN A 385 85.367 −9.925 8.043 1.00 20.00 2100 OD1 ASN A 385 86.415 −10.419 7.638 1.00 20.00 2101 ND2 ASN A 385 84.535 −9.219 7.259 1.00 20.00 2102 N GLY A 386 88.171 −10.355 11.286 1.00 20.00 2103 CA GLY A 386 89.376 −9.584 11.526 1.00 20.00 2104 C GLY A 386 89.506 −8.487 12.584 1.00 20.00 2105 O GLY A 386 90.579 −7.957 12.839 1.00 20.00 2106 N THR A 387 88.331 −8.168 13.157 1.00 38.04 2107 CA THR A 387 88.344 −7.159 14.198 1.00 34.81 2108 C THR A 387 87.955 −7.470 15.656 1.00 29.35 2109 O THR A 387 86.789 −7.590 16.010 1.00 25.60 2110 CB THR A 387 87.528 −5.883 13.919 1.00 35.26 2111 OG1 THR A 387 88.115 −5.484 12.678 1.00 38.62 2112 CG2 THR A 387 87.395 −4.652 14.820 1.00 35.18 2113 N THR A 388 88.985 −7.660 16.494 1.00 25.85 2114 CA THR A 388 88.710 −8.130 17.839 1.00 22.57 2115 C THR A 388 88.537 −6.958 18.802 1.00 23.19 2116 O THR A 388 89.230 −5.952 18.738 1.00 19.61 2117 CB THR A 388 89.885 −9.000 18.298 1.00 23.33 2118 OG1 THR A 388 90.119 −10.030 17.334 1.00 21.46 2119 CG2 THR A 388 89.580 −9.641 19.654 1.00 22.30 2120 N GLN A 389 87.527 −7.200 19.658 1.00 22.43 2121 CA GLN A 389 87.071 −6.338 20.720 1.00 22.51 2122 C GLN A 389 86.719 −7.159 21.964 1.00 20.76 2123 O GLN A 389 86.488 −8.371 21.900 1.00 19.22 2124 CB GLN A 389 85.816 −5.511 20.338 1.00 24.03 2125 CG GLN A 389 85.999 −4.637 19.092 1.00 24.14 2126 CD GLN A 389 84.826 −3.772 18.742 1.00 25.61 2127 OE1 GLN A 389 84.635 −2.750 19.381 1.00 25.60 2128 NE2 GLN A 389 83.968 −4.122 17.762 1.00 26.31 2129 N THR A 390 86.593 −6.495 23.107 1.00 20.02 2130 CA THR A 390 86.149 −7.117 24.347 1.00 17.35 2131 C THR A 390 84.749 −6.591 24.716 1.00 18.81 2132 O THR A 390 84.358 −5.465 24.384 1.00 17.69 2133 CB THR A 390 87.071 −6.834 25.557 1.00 17.85 2134 OG1 THR A 390 87.007 −5.414 25.809 1.00 18.20 2135 CG2 THR A 390 88.505 −7.265 25.256 1.00 17.70 2136 N ALA A 391 84.004 −7.388 25.445 1.00 17.61 2137 CA ALA A 391 82.657 −7.095 25.890 1.00 18.43 2138 C ALA A 391 82.254 −7.783 27.192 1.00 17.62 2139 O ALA A 391 82.712 −8.896 27.470 1.00 17.18 2140 CB ALA A 391 81.673 −7.613 24.811 1.00 16.39 2141 N VAL A 392 81.382 −7.128 27.942 1.00 17.34 2142 CA VAL A 392 80.822 −7.676 29.180 1.00 15.98 2143 C VAL A 392 79.722 −8.661 28.776 1.00 15.84 2144 O VAL A 392 79.002 −8.376 27.793 1.00 16.85 2145 CB VAL A 392 80.205 −6.584 30.070 1.00 15.95 2146 CG1 VAL A 392 79.490 −7.180 31.301 1.00 15.89 2147 CG2 VAL A 392 81.266 −5.543 30.482 1.00 15.39 2148 N ASP A 393 79.650 −9.799 29.422 1.00 15.45 2149 CA ASP A 393 78.587 −10.790 29.162 1.00 16.16 2150 C ASP A 393 77.217 −10.175 29.367 1.00 15.39 2151 O ASP A 393 76.864 −9.706 30.471 1.00 14.42 2152 CB ASP A 393 78.802 −11.946 30.158 1.00 14.87 2153 CG ASP A 393 78.031 −13.211 29.948 1.00 16.08 2154 OD1 ASP A 393 78.506 −14.295 30.403 1.00 16.54 2155 OD2 ASP A 393 76.950 −13.261 29.285 1.00 17.16 2156 N PRO A 394 76.340 −10.247 28.378 1.00 16.89 2157 CA PRO A 394 74.976 −9.706 28.510 1.00 18.08 2158 C PRO A 394 74.160 −10.345 29.626 1.00 17.40 2159 O PRO A 394 73.183 −9.757 30.116 1.00 17.22 2160 CB PRO A 394 74.341 −9.948 27.148 1.00 16.39 2161 CG PRO A 394 75.545 −9.916 26.223 1.00 18.52 2162 CD PRO A 394 76.619 −10.675 26.975 1.00 17.04 2163 N TYR A 395 74.517 −11.568 30.006 1.00 16.37 2164 CA TYR A 395 73.877 −12.321 31.086 1.00 16.64 2165 C TYR A 395 74.578 −12.142 32.436 1.00 16.49 2166 O TYR A 395 74.184 −12.763 33.421 1.00 15.61 2167 CB TYR A 395 73.809 −13.820 30.721 1.00 16.31 2168 CG TYR A 395 72.739 −14.174 29.709 1.00 14.68 2169 CD1 TYR A 395 71.590 −14.846 30.151 1.00 16.46 2170 CD2 TYR A 395 72.836 −13.825 28.360 1.00 14.83 2171 CE1 TYR A 395 70.576 −15.175 29.276 1.00 13.85 2172 CE2 TYR A 395 71.820 −14.169 27.441 1.00 14.80 2173 CZ TYR A 395 70.691 −14.792 27.935 1.00 15.21 2174 OH TYR A 395 69.637 −15.146 27.113 1.00 15.56 2175 N ALA A 396 75.632 −11.307 32.568 1.00 16.64 2176 CA ALA A 396 76.260 −11.116 33.880 1.00 17.32 2177 C ALA A 396 75.211 −10.694 34.933 1.00 18.30 2178 O ALA A 396 74.298 −9.914 34.629 1.00 15.51 2179 CB ALA A 396 77.260 −9.939 33.770 1.00 17.84 2180 N ARG A 397 75.388 −11.057 36.198 1.00 16.48 2181 CA ARG A 397 74.538 −10.729 37.300 1.00 15.87 2182 C ARG A 397 75.103 −9.694 38.274 1.00 18.12 2183 O ARG A 397 74.380 −9.284 39.196 1.00 15.59 2184 CB ARG A 397 74.185 −12.040 38.027 1.00 18.60 2185 CG ARG A 397 73.784 −13.316 37.287 1.00 19.84 2186 CD ARG A 397 72.553 −13.420 36.379 1.00 24.90 2187 NE ARG A 397 72.208 −14.621 35.612 1.00 22.76 2188 CZ ARG A 397 71.025 −14.402 35.008 1.00 23.41 2189 NH1 ARG A 397 70.886 −13.392 34.144 1.00 19.94 2190 NH2 ARG A 397 70.123 −15.367 35.053 1.00 23.58 2191 N ALA A 398 76.346 −9.296 38.010 1.00 16.37 2192 CA ALA A 398 77.067 −8.350 38.855 1.00 17.06 2193 C ALA A 398 78.247 −7.820 38.038 1.00 15.40 2194 O ALA A 398 78.597 −8.413 37.006 1.00 15.82 2195 CB ALA A 398 77.565 −9.054 40.119 1.00 16.67 2196 N ILE A 399 78.785 −6.669 38.345 1.00 15.06 2197 CA ILE A 399 79.836 −6.039 37.572 1.00 15.89 2198 C ILE A 399 80.901 −5.366 38.448 1.00 17.93 2199 O ILE A 399 80.735 −5.221 39.663 1.00 15.09 2200 CB ILE A 399 79.242 −4.896 36.717 1.00 15.87 2201 CG1 ILE A 399 78.242 −4.078 37.530 1.00 16.12 2202 CG2 ILE A 399 78.528 −5.438 35.467 1.00 18.19 2203 CD1 ILE A 399 77.845 −2.740 36.574 1.00 16.62 2204 N SER A 400 81.929 −4.847 37.736 1.00 16.57 2205 CA SER A 400 82.921 −3.993 38.409 1.00 15.56 2206 C SER A 400 82.236 −2.619 38.438 1.00 17.27 2207 O SER A 400 81.271 −2.466 37.653 1.00 16.46 2208 CB SER A 400 84.181 −3.946 37.561 1.00 15.65 2209 OG SER A 400 83.953 −3.310 36.304 1.00 15.40 2210 N VAL A 401 82.765 −1.616 39.082 1.00 15.63 2211 CA VAL A 401 82.217 −0.260 39.027 1.00 16.67 2212 C VAL A 401 82.096 0.223 37.617 1.00 18.39 2213 O VAL A 401 83.057 0.177 36.827 1.00 19.89 2214 CB VAL A 401 83.072 0.692 39.881 1.00 17.74 2215 CG1 VAL A 401 82.552 2.095 39.678 1.00 16.22 2216 CG2 VAL A 401 83.009 0.220 41.367 1.00 16.84 2217 N ASN A 402 80.936 0.785 37.203 1.00 19.45 2218 CA ASN A 402 80.780 1.251 35.824 1.00 19.83 2219 C ASN A 402 80.895 0.145 34.794 1.00 19.97 2220 O ASN A 402 81.048 0.448 33.599 1.00 19.00 2221 CB ASN A 402 81.846 2.355 35.598 1.00 19.30 2222 CG ASN A 402 51.421 3.707 36.135 1.00 19.90 2223 OD1 ASN A 402 82.255 4.564 36.508 1.00 22.70 2224 ND2 ASN A 402 80.134 3.976 36.206 1.00 13.99 2225 N ALA A 403 80.760 −1.136 35.122 1.00 19.56 2226 CA ALA A 403 80.744 −2.240 34.195 1.00 19.22 2227 C ALA A 403 81.897 −2.271 33.197 1.00 20.03 2228 O ALA A 403 81.731 −2.512 31.990 1.00 19.77 2229 CB ALA A 403 79.404 −2.200 33.423 1.00 19.35 2230 N THR A 404 83.131 −2.081 33.640 1.00 19.82 2231 CA THR A 404 84.301 −2.251 32.776 1.00 18.92 2232 C THR A 404 84.452 −3.747 32.583 1.00 19.28 2233 O THR A 404 85.132 −4.210 31.650 1.00 19.93 2234 CB THR A 404 85.587 −1.740 33.443 1.00 19.67 2235 OG1 THR A 404 85.795 −2.458 34.677 1.00 17.98 2236 CG2 THR A 404 85.515 −0.275 33.830 1.00 19.70 2237 N ARG A 405 83.995 −4.583 33.519 1.00 18.67 2238 CA ARG A 405 84.057 −6.024 33.509 1.00 16.48 2239 C ARG A 405 82.819 −6.658 34.168 1.00 17.16 2240 O ARG A 405 82.173 −5.960 34.970 1.00 16.14 2241 CB ARG A 405 85.261 −6.496 34.398 1.00 17.15 2242 CG ARG A 405 86.612 −5.917 33.939 1.00 17.89 2243 CD ARG A 405 87.772 −6.025 34.923 1.00 18.82 2244 NE ARG A 405 88.953 −5.382 34.421 1.00 18.77 2245 CZ ARG A 405 90.220 −5.421 34.908 1.00 19.96 2246 NH1 ARG A 405 90.555 −6.060 36.027 1.00 17.06 2247 NH2 ARG A 405 91.142 −4.729 34.232 1.00 19.62 2248 N GLY A 406 82.544 −7.922 33.884 1.00 15.61 2249 CA GLY A 406 81.431 −8.620 34.562 1.00 16.45 2250 C GLY A 406 82.102 −9.320 35.780 1.00 18.96 2251 O GLY A 406 83.334 −9.449 35.807 1.00 16.60 2252 N MET A 407 81.317 −9.686 36.773 1.00 18.47 2253 CA MET A 407 81.762 −10.295 38.010 1.00 18.88 2254 C MET A 407 81.015 −11.578 38.326 1.00 18.40 2255 O MET A 407 79.775 −11.615 38.240 1.00 17.72 2256 CB MET A 407 81.542 −9.323 39.182 1.00 18.65 2257 CG MET A 407 82.166 −9.673 40.526 1.00 16.86 2258 SD MET A 407 81.647 −8.523 41.829 1.00 16.73 2259 CE MET A 407 82.557 −9.127 43.234 1.00 19.44 2260 N ILE A 408 81.750 −12.645 38.616 1.00 16.52 2261 CA ILE A 408 81.201 −13.950 38.956 1.00 14.94 2262 C ILE A 408 80.888 −13.997 40.454 1.00 18.17 2263 O ILE A 408 81.786 −13.697 41.268 1.00 19.12 2264 CB ILE A 408 82.249 −15.018 38.606 1.00 15.45 2265 CG1 ILE A 408 82.565 −15.005 37.081 1.00 15.33 2266 CG2 ILE A 408 81.742 −16.389 39.050 1.00 16.59 2267 CD1 ILE A 408 84.051 −15.308 36.771 1.00 17.24 2268 N VAL A 409 79.647 −14.260 40.875 1.00 16.48 2269 CA VAL A 409 79.309 −14.206 42.292 1.00 18.09 2270 C VAL A 409 78.466 −15.386 42.736 1.00 19.37 2271 O VAL A 409 77.906 −16.108 41.930 1.00 20.30 2272 CB VAL A 409 78.544 −12.920 42.668 1.00 17.54 2273 CG1 VAL A 409 79.352 −11.657 42.436 1.00 14.93 2274 CG2 VAL A 409 77.237 −12.727 41.871 1.00 18.02 2275 N ASP A 410 78.372 −15.587 44.041 1.00 21.46 2276 CA ASP A 410 77.548 −16.630 44.651 1.00 23.20 2277 C ASP A 410 76.213 −15.995 45.035 1.00 22.82 2278 O ASP A 410 76.182 −15.290 46.065 1.00 22.94 2279 CB ASP A 410 78.239 −17.131 45.946 1.00 23.65 2280 CG ASP A 410 77.474 −18.262 46.611 1.00 24.86 2281 OD1 ASP A 410 76.311 −18.535 46.249 1.00 25.50 2282 OD2 ASP A 410 78.060 −18.934 47.490 1.00 27.15 2283 N LEU A 411 75.146 −16.167 44.271 1.00 21.42 2284 CA LEU A 411 73.882 −15.508 44.506 1.00 21.38 2285 C LEU A 411 73.237 −15.851 45.845 1.00 22.44 2286 O LEU A 411 72.566 −14.989 46.436 1.00 19.95 2287 CB LEU A 411 72.876 −15.820 43.360 1.00 20.60 2288 CG LEU A 411 73.222 −15.156 42.010 1.00 20.02 2289 CD1 LEU A 411 72.363 −15.723 40.902 1.00 16.46 2290 CD2 LEU A 411 73.133 −13.644 42.152 1.00 19.54 2291 N LYS A 412 73.415 −17.079 46.331 1.00 21.58 2292 CA LYS A 412 72.795 −17.452 47.612 1.00 22.40 2293 C LYS A 412 73.254 −16.679 48.824 1.00 22.02 2294 O LYS A 412 72.506 −16.191 49.703 1.00 22.52 2295 CB LYS A 412 73.028 −18.966 47.842 1.00 26.92 2296 CG LYS A 412 72.311 −19.472 49.084 1.00 31.49 2297 CD LYS A 412 70.825 −19.669 48.788 1.00 33.84 2298 CE LYS A 412 70.110 −19.953 50.118 1.00 37.42 2299 NZ LYS A 412 70.382 −18.751 50.970 1.00 40.45 2300 N ALA A 413 74.517 −16.248 48.810 1.00 18.93 2301 CA ALA A 413 75.194 −15.455 49.803 1.00 20.77 2302 C ALA A 413 74.716 −14.003 49.860 1.00 20.66 2303 O ALA A 413 74.909 −13.273 50.842 1.00 21.58 2304 CB ALA A 413 76.696 −15.412 49.507 1.00 19.90 2305 N THR A 414 74.083 −13.550 48.779 1.00 19.42 2306 CA THR A 414 73.566 −12.207 48.706 1.00 20.42 2307 C THR A 414 72.181 −12.039 49.330 1.00 22.20 2308 O THR A 414 71.750 −10.883 49.514 1.00 20.49 2309 CB THR A 414 73.489 −11.665 47.263 1.00 20.49 2310 OG1 THR A 414 72.430 −12.401 46.619 1.00 21.35 2311 CG2 THR A 414 74.770 −11.821 46.451 1.00 19.00 2312 N ASP A 415 71.470 −13.097 49.627 1.00 21.64 2313 CA ASP A 415 70.149 −13.115 50.208 1.00 21.34 2314 C ASP A 415 70.129 −12.642 51.661 1.00 20.48 2315 O ASP A 415 70.955 −13.100 52.457 1.00 21.23 2316 CB ASP A 415 69.544 −14.522 50.278 1.00 21.16 2317 CG ASP A 415 69.327 −15.177 48.937 1.00 23.55 2318 OD1 ASP A 415 69.131 −14.545 47.881 1.00 22.11 2319 OD2 ASP A 415 69.342 −16.414 48.905 1.00 24.37 2320 N PRO A 416 69.298 −11.654 51.921 1.00 18.99 2321 CA PRO A 416 69.131 −11.131 53.268 1.00 18.59 2322 C PRO A 416 68.487 −12.203 54.143 1.00 19.83 2323 O PRO A 416 67.848 −13.131 53.613 1.00 16.95 2324 CB PRO A 416 68.177 −9.955 53.092 1.00 18.50 2325 CG PRO A 416 67.383 −10.255 51.848 1.00 18.19 2326 CD PRO A 416 68.355 −11.017 50.963 1.00 18.15 2327 N ALA A 417 68.584 −12.001 55.459 1.00 19.41 2328 CA ALA A 417 67.928 −12.898 56.410 1.00 18.88 2329 C ALA A 417 66.416 −12.866 56.226 1.00 19.84 2330 O ALA A 417 65.795 −11.828 55.964 1.00 19.83 2331 CB ALA A 417 68.258 −12.437 57.822 1.00 18.37 2332 N GLY A 418 65.790 −14.020 56.379 1.00 21.41 2333 CA GLY A 418 64.368 −14.233 56.237 1.00 23.22 2334 C GLY A 418 63.846 −14.337 54.810 1.00 23.60 2335 O GLY A 418 62.643 −14.572 54.590 1.00 22.08 2336 N TRP A 419 64.710 −14.183 53.807 1.00 23.46 2337 CA TRP A 419 64.402 −14.234 52.396 1.00 23.20 2338 C TRP A 419 63.606 −15.472 52.012 1.00 25.42 2339 O TRP A 419 62.668 −15.373 51.199 1.00 24.03 2340 CB TRP A 419 65.670 −14.233 51.530 1.00 22.84 2341 CG TRP A 419 65.454 −13.984 50.043 1.00 22.68 2342 CD1 TRP A 419 65.788 −14.816 48.989 1.00 21.27 2343 CD2 TRP A 419 64.806 −12.860 49.459 1.00 20.14 2344 NE1 TRP A 419 65.454 −14.166 47.813 1.00 22.72 2345 CE2 TRP A 419 64.841 −12.969 48.060 1.00 21.05 2346 CE3 TRP A 419 64.233 −11.704 50.009 1.00 21.41 2347 CZ2 TRP A 419 64.305 −12.027 47.163 1.00 20.75 2348 CZ3 TRP A 419 63.711 −10.769 49.147 1.00 22.68 2349 CH2 TRP A 419 63.761 −10.889 47.753 1.00 21.75 2350 N GLN A 420 63.929 −16.638 52.581 1.00 26.47 2351 CA GLN A 420 63.179 −17.861 52.325 1.00 29.80 2352 C GLN A 420 61.719 −17.770 52.728 1.00 28.92 2353 O GLN A 420 60.919 −18.452 52.090 1.00 28.66 2354 CB GLN A 420 63.849 −19.089 52.961 1.00 33.14 2355 CG GLN A 420 64.919 −19.737 52.090 1.00 39.56 2356 CD GLN A 420 64.607 −19.919 50.614 1.00 41.28 2357 OE1 GLN A 420 65.071 −19.074 49.835 1.00 43.54 2358 NE2 GLN A 420 63.849 −20.928 50.243 1.00 43.71 2359 N GLY A 421 61.326 −16.936 53.690 1.00 29.02 2360 CA GLY A 421 59.929 −16.790 54.080 1.00 27.43 2361 C GLY A 421 59.223 −15.673 53.308 1.00 28.32 2362 O GLY A 421 58.048 −15.418 53.556 1.00 24.66 2363 N ASP A 422 59.878 −15.004 52.358 1.00 28.80 2364 CA ASP A 422 59.295 −13.889 51.627 1.00 30.89 2365 C ASP A 422 58.088 −14.200 50.738 1.00 36.19 2366 O ASP A 422 58.230 −14.870 49.727 1.00 38.46 2367 CB ASP A 422 60.420 −13.227 50.804 1.00 27.10 2368 CG ASP A 422 59.951 −11.980 50.032 1.00 25.30 2369 OD1 ASP A 422 59.222 −11.152 50.594 1.00 23.55 2370 OD2 ASP A 422 60.287 −11.929 48.830 1.00 22.98 2371 N HIS A 423 56.911 −13.629 51.020 1.00 40.93 2372 CA HIS A 423 55.703 −13.849 50.233 1.00 47.21 2373 C HIS A 423 55.313 −12.763 49.209 1.00 45.35 2374 O HIS A 423 54.768 −11.681 49.406 1.00 47.07 2375 CB HIS A 423 54.512 −14.100 51.176 1.00 51.41 2376 CG HIS A 423 53.238 −14.617 50.601 1.00 56.21 2377 ND1 HIS A 423 52.275 −13.795 50.033 1.00 58.05 2378 CD2 HIS A 423 52.745 −15.896 50.562 1.00 57.47 2379 CE1 HIS A 423 51.265 −14.568 49.639 1.00 58.60 2380 NE2 HIS A 423 51.519 −15.838 49.939 1.00 58.38 2381 N GLU A 424 55.414 −13.228 47.961 1.00 43.93 2382 CA GLU A 424 54.955 −12.662 46.717 1.00 41.46 2383 C GLU A 424 53.561 −12.097 47.029 1.00 35.89 2384 O GLU A 424 52.765 −12.666 47.764 1.00 32.50 2385 CB GLU A 424 54.860 −13.614 45.537 1.00 45.39 2386 CG GLU A 424 53.602 −14.436 45.385 1.00 50.15 2387 CD GLU A 424 53.588 −15.845 45.929 1.00 53.14 2388 OE1 GLU A 424 52.472 −16.435 45.889 1.00 55.07 2389 OE2 GLU A 424 54.628 −16.378 46.392 1.00 54.61 2390 N GLN A 425 53.341 −10.927 46.478 1.00 31.51 2391 CA GLN A 425 52.114 −10.187 46.730 1.00 30.43 2392 C GLN A 425 51.336 −9.895 45.465 1.00 27.84 2393 O GLN A 425 51.444 −8.806 44.889 1.00 25.73 2394 CB GLN A 425 52.513 −8.862 47.412 1.00 28.91 2395 CG GLN A 425 52.923 −9.100 48.863 1.00 31.80 2396 CD GLN A 425 51.701 −9.408 49.711 1.00 34.90 2397 OE1 GLN A 425 51.857 −10.238 50.604 1.00 35.50 2398 NE2 GLN A 425 50.583 −8.779 49.384 1.00 34.92 2399 N THR A 426 50.650 −10.924 44.981 1.00 25.79 2400 CA THR A 426 49.878 −10.700 43.722 1.00 25.43 2401 C THR A 426 48.438 −11.054 44.030 1.00 24.91 2402 O THR A 426 48.194 −12.077 44.673 1.00 25.67 2403 CB THR A 426 50.462 −11.587 42.625 1.00 24.59 2404 OG1 THR A 426 50.660 −12.926 43.104 1.00 26.94 2405 CG2 THR A 426 51.843 −11.146 42.152 1.00 25.00 2406 N PRO A 427 47.481 −10.229 43.662 1.00 24.58 2407 CA PRO A 427 46.078 −10.493 43.995 1.00 22.44 2408 C PRO A 427 45.481 −11.448 42.987 1.00 19.97 2409 O PRO A 427 46.143 −11.846 42.015 1.00 18.98 2410 CB PRO A 427 45.449 −9.098 43.970 1.00 22.44 2411 CG PRO A 427 46.215 −8.410 42.886 1.00 23.34 2412 CD PRO A 427 47.643 −8.943 42.956 1.00 24.22 2413 N ALA A 428 44.221 −11.818 43.186 1.00 18.32 2414 CA ALA A 428 43.524 −12.705 42.287 1.00 18.67 2415 C ALA A 428 43.302 −12.115 40.901 1.00 18.67 2416 O ALA A 428 43.391 −12.950 39.990 1.00 18.53 2417 CB ALA A 428 42.176 −13.179 42.853 1.00 19.42 2418 N ASN A 429 43.248 −10.788 40.730 1.00 16.60 2419 CA ASN A 429 43.080 −10.263 39.358 1.00 15.96 2420 C ASN A 429 43.673 −8.877 39.366 1.00 16.94 2421 O ASN A 429 43.676 −8.221 40.413 1.00 17.66 2422 CB ASN A 429 41.572 −10.199 39.015 1.00 15.37 2423 CG ASN A 429 41.218 −9.874 37.587 1.00 14.52 2424 OD1 ASN A 429 40.864 −10.725 36.749 1.00 17.02 2425 ND2 ASN A 429 41.224 −8.619 37.164 1.00 12.11 2426 N PRO A 430 44.223 −8.379 38.259 1.00 17.36 2427 CA PRO A 430 44.798 −7.059 38.201 1.00 17.36 2428 C PRO A 430 43.884 −5.954 38.671 1.00 16.98 2429 O PRO A 430 44.439 −4.967 39.171 1.00 15.58 2430 CB PRO A 430 45.274 −6.889 36.756 1.00 17.72 2431 CG PRO A 430 45.459 −8.315 36.305 1.00 17.97 2432 CD PRO A 430 44.377 −9.110 36.977 1.00 16.18 2433 N VAL A 431 42.554 −5.999 38.575 1.00 16.77 2434 CA VAL A 431 41.696 −4.882 39.029 1.00 14.93 2435 C VAL A 431 41.724 −4.718 40.549 1.00 16.96 2436 O VAL A 431 41.207 −3.711 41.066 1.00 14.24 2437 CB VAL A 431 40.236 −5.000 38.552 1.00 14.61 2438 CG1 VAL A 431 40.141 −5.164 37.018 1.00 11.37 2439 CG2 VAL A 431 39.470 −6.174 39.204 1.00 9.63 2440 N ASP A 432 42.285 −5.672 41.303 1.00 15.55 2441 CA ASP A 432 42.506 −5.572 42.728 1.00 16.35 2442 C ASP A 432 43.735 −4.744 43.102 1.00 16.54 2443 O ASP A 432 43.956 −4.499 44.305 1.00 15.51 2444 CB ASP A 432 42.669 −6.988 43.365 1.00 14.88 2445 CG ASP A 432 41.447 −7.835 43.087 1.00 15.34 2446 OD1 ASP A 432 40.318 −7.267 43.043 1.00 16.21 2447 OD2 ASP A 432 41.488 −9.064 42.873 1.00 14.61 2448 N GLU A 433 44.537 −4.259 42.145 1.00 15.94 2449 CA GLU A 433 45.689 −3.429 42.512 1.00 16.94 2450 C GLU A 433 45.343 −1.946 42.441 1.00 16.06 2451 O GLU A 433 44.479 −1.513 41.664 1.00 16.07 2452 CB GLU A 433 46.942 −3.630 41.625 1.00 15.85 2453 CG GLU A 433 47.546 −5.015 41.739 1.00 16.52 2454 CD GLU A 433 48.933 −5.312 41.195 1.00 16.36 2455 OE1 GLU A 433 49.492 −4.536 40.379 1.00 11.53 2456 OE2 GLU A 433 49.449 −6.397 41.635 1.00 14.91 2457 N VAL A 434 46.021 −1.168 43.262 1.00 15.28 2458 CA VAL A 434 46.036 0.299 43.193 1.00 14.14 2459 C VAL A 434 47.553 0.628 43.106 1.00 15.28 2460 O VAL A 434 48.292 0.509 44.136 1.00 13.41 2461 CB VAL A 434 45.360 0.930 44.419 1.00 14.74 2462 CG1 VAL A 434 45.241 2.440 44.130 1.00 14.68 2463 CG2 VAL A 434 43.954 0.334 44.672 1.00 13.12 2464 N ILE A 435 48.014 1.058 41.947 1.00 14.64 2465 CA ILE A 435 49.459 1.202 41.665 1.00 13.40 2466 C ILE A 435 49.966 2.607 41.870 1.00 15.38 2467 O ILE A 435 49.312 3.525 41.385 1.00 17.74 2468 CB ILE A 435 49.775 0.758 40.228 1.00 14.42 2469 CG1 ILE A 435 49.243 0.693 40.023 1.00 14.98 2470 CG2 ILE A 435 51.253 0.888 39.874 1.00 12.09 2471 CD1 ILE A 435 49.227 −1.169 38.568 1.00 13.44 2472 N TYR A 436 51.082 2.759 42.563 1.00 13.59 2473 CA TYR A 436 51.698 4.037 42.855 1.00 15.25 2474 C TYR A 436 53.109 4.093 42.264 1.00 15.01 2475 O TYR A 436 53.988 3.279 42.617 1.00 14.02 2476 CB TYR A 436 51.711 4.156 44.367 1.00 15.52 2477 CG TYR A 436 52.196 5.355 45.116 1.00 16.16 2478 CD1 TYR A 436 51.289 6.303 45.576 1.00 15.41 2479 CD2 TYR A 436 53.549 5.498 45.460 1.00 15.75 2480 CE1 TYR A 436 51.717 7.384 46.327 1.00 16.02 2481 CE2 TYR A 436 53.987 6.584 46.218 1.00 15.63 2482 CZ TYR A 436 53.058 7.496 46.674 1.00 15.39 2483 OH TYR A 436 53.434 8.562 47.464 1.00 16.13 2484 N GLU A 437 53.329 4.992 41.304 1.00 15.46 2485 CA GLU A 437 54.622 5.123 40.620 1.00 15.46 2486 C GLU A 437 55.651 5.927 41.411 1.00 16.03 2487 O GLU A 437 55.329 7.076 41.747 1.00 17.07 2488 CB GLU A 437 54.458 5.834 39.263 1.00 15.08 2489 CG GLU A 437 55.716 5.978 38.411 1.00 14.65 2490 CD GLU A 437 55.493 6.596 37.048 1.00 14.65 2491 OE1 GLU A 437 54.648 7.489 36.869 1.00 15.22 2492 OE2 GLU A 437 56.087 6.145 36.035 1.00 16.08 2493 N ALA A 438 56.882 5.394 41.543 1.00 13.82 2494 CA ALA A 438 57.878 6.186 42.253 1.00 13.55 2495 C ALA A 438 59.312 5.910 41.823 1.00 14.91 2496 O ALA A 438 59.721 4.775 41.558 1.00 13.87 2497 CB ALA A 438 57.660 5.898 43.765 1.00 13.69 2498 N HIS A 439 60.142 6.969 41.828 1.00 16.29 2499 CA HIS A 439 61.572 6.838 41.501 1.00 16.19 2500 C HIS A 439 62.351 6.603 42.805 1.00 16.70 2501 O HIS A 439 62.025 7.212 43.813 1.00 14.31 2502 CB HIS A 439 62.043 8.086 40.776 1.00 16.30 2503 CG HIS A 439 63.440 8.147 40.223 1.00 16.75 2504 ND1 HIS A 439 64.518 8.470 41.049 1.00 15.99 2505 CD2 HIS A 439 63.943 7.963 38.965 1.00 14.58 2506 CE1 HIS A 439 65.624 8.516 40.288 1.00 17.06 2507 NE2 HIS A 439 65.302 8.221 39.029 1.00 16.41 2508 N VAL A 440 63.328 5.687 42.858 1.00 15.20 2509 CA VAL A 440 64.031 5.389 44.106 1.00 15.25 2510 C VAL A 440 64.653 6.618 44.780 1.00 16.03 2511 O VAL A 440 64.516 6.773 45.999 1.00 16.04 2512 CB VAL A 440 65.116 4.317 43.867 1.00 15.02 2513 CG1 VAL A 440 65.972 4.169 45.128 1.00 16.66 2514 CG2 VAL A 440 64.459 2.977 43.508 1.00 15.14 2515 N ARG A 441 65.342 7.469 44.034 1.00 16.63 2516 CA ARG A 441 65.925 8.698 44.541 1.00 17.10 2517 C ARG A 441 64.899 9.740 45.000 1.00 17.55 2518 O ARG A 441 65.010 10.221 46.170 1.00 17.74 2519 CB ARG A 441 66.896 9.304 43.501 1.00 14.61 2520 CG ARG A 441 67.704 10.461 44.088 1.00 16.94 2521 CD ARG A 441 68.732 11.060 43.137 1.00 18.60 2522 NE ARG A 441 69.386 12.271 43.671 1.00 16.23 2523 CZ ARG A 441 70.470 12.234 44.458 1.00 17.59 2524 NH1 ARG A 441 71.094 11.121 44.855 1.00 17.67 2525 NH2 ARG A 441 71.002 13.363 44.893 1.00 17.22 2526 N ASP A 442 63.897 10.087 44.191 1.00 16.68 2527 CA ASP A 442 62.882 11.067 44.550 1.00 17.07 2528 C ASP A 442 62.150 10.781 45.865 1.00 15.50 2529 O ASP A 442 61.789 11.686 46.627 1.00 14.92 2530 CB ASP A 442 61.705 11.140 43.534 1.00 16.09 2531 CG ASP A 442 62.092 11.481 42.103 1.00 18.27 2532 OD1 ASP A 442 61.161 11.472 41.265 1.00 16.61 2533 OD2 ASP A 442 63.293 11.722 41.820 1.00 16.36 2534 N PHE A 443 61.865 9.519 46.113 1.00 14.50 2535 CA PHE A 443 61.090 9.094 47.277 1.00 14.57 2536 C PHE A 443 61.629 9.580 48.615 1.00 16.96 2537 O PHE A 443 60.820 9.958 49.474 1.00 15.43 2538 CB PHE A 443 61.104 7.553 47.333 1.00 15.23 2539 CG PHE A 443 60.077 7.005 48.292 1.00 16.07 2540 CD1 PHE A 443 60.475 6.290 49.410 1.00 17.87 2541 CD2 PHE A 443 58.722 7.225 48.081 1.00 17.50 2542 CE1 PHE A 443 59.546 5.788 50.302 1.00 19.15 2543 CE2 PHE A 443 57.797 6.682 48.961 1.00 19.87 2544 CZ PHE A 443 58.202 5.978 50.077 1.00 19.27 2545 N SER A 444 62.941 9.578 48.844 1.00 14.65 2546 CA SER A 444 63.491 10.014 50.121 1.00 16.85 2547 C SER A 444 64.692 10.959 50.081 1.00 17.60 2548 O SER A 444 65.223 11.288 51.168 1.00 17.78 2549 CB SER A 444 63.933 8.772 50.891 1.00 17.91 2550 OG SER A 444 64.813 8.072 50.004 1.00 18.93 2551 N ILE A 445 65.083 11.532 48.944 1.00 16.65 2552 CA ILE A 445 66.272 12.363 48.864 1.00 17.86 2553 C ILE A 445 66.133 13.664 49.641 1.00 19.05 2554 O ILE A 445 67.136 14.236 50.089 1.00 19.84 2555 CB ILE A 445 66.725 12.704 47.422 1.00 18.82 2556 CG1 ILE A 445 68.114 13.345 47.373 1.00 19.76 2557 CG2 ILE A 445 65.717 13.625 46.737 1.00 16.03 2558 CD1 ILE A 445 69.261 12.451 47.830 1.00 17.68 2559 N ASP A 446 64.944 14.247 49.757 1.00 17.88 2560 CA ASP A 446 64.795 15.549 50.429 1.00 19.31 2561 C ASP A 446 65.343 15.527 51.856 1.00 18.39 2562 O ASP A 446 65.028 14.618 52.664 1.00 14.79 2563 CB ASP A 446 63.319 15.965 50.406 1.00 17.77 2564 CG ASP A 446 62.997 17.404 50.598 1.00 19.68 2565 OD1 ASP A 446 62.211 18.007 49.823 1.00 20.47 2566 OD2 ASP A 446 63.527 18.071 51.516 1.00 17.16 2567 N ALA A 447 65.955 16.640 52.293 1.00 19.59 2568 CA ALA A 447 66.372 16.734 53.696 1.00 20.17 2569 C ALA A 447 65.212 16.578 54.680 1.00 21.62 2570 O ALA A 447 65.444 16.179 55.845 1.00 20.80 2571 CB ALA A 447 67.086 18.077 53.958 1.00 22.60 2572 N ASN A 448 63.958 16.873 54.328 1.00 20.17 2573 CA ASN A 448 62.852 16.752 55.303 1.00 19.49 2574 C ASN A 448 62.130 15.408 55.274 1.00 20.38 2575 O ASN A 448 61.062 15.275 55.906 1.00 18.16 2576 CB ASN A 448 61.835 17.863 54.959 1.00 18.25 2577 CG ASN A 448 61.103 17.701 53.619 1.00 19.72 2578 OD1 ASN A 448 61.019 16.634 52.997 1.00 19.01 2579 ND2 ASN A 448 60.625 18.786 53.028 1.00 18.34 2580 N SER A 449 62.630 14.404 54.537 1.00 19.41 2581 CA SER A 449 61.917 13.131 54.370 1.00 20.28 2582 C SER A 449 61.780 12.255 55.599 1.00 20.00 2583 O SER A 449 60.950 11.332 55.677 1.00 20.48 2584 CB SER A 449 62.563 12.336 53.203 1.00 18.80 2585 OG SER A 449 63.731 11.616 53.593 1.00 16.39 2586 N GLY A 450 62.709 12.410 56.516 1.00 19.28 2587 CA GLY A 450 62.812 11.662 57.762 1.00 18.69 2588 C GLY A 450 63.495 10.312 57.606 1.00 19.34 2589 O GLY A 450 63.580 9.532 58.586 1.00 19.10 2590 N MET A 451 63.897 9.939 56.412 1.00 17.66 2591 CA MET A 451 64.550 8.650 56.169 1.00 19.49 2592 C MET A 451 66.056 8.859 56.152 1.00 21.41 2593 O MET A 451 66.534 9.886 55.659 1.00 21.59 2594 CB MET A 451 64.044 8.109 54.818 1.00 18.54 2595 CG MET A 451 62.704 7.387 54.938 1.00 18.74 2596 SD MET A 451 61.951 7.071 53.330 1.00 15.90 2597 CE MET A 451 61.313 8.726 52.990 1.00 16.43 2598 N LYS A 452 66.849 7.964 56.728 1.00 24.96 2599 CA LYS A 452 68.292 8.105 56.755 1.00 25.67 2600 C LYS A 452 69.007 7.729 55.462 1.00 24.98 2601 O LYS A 452 69.976 8.421 55.111 1.00 22.58 2602 CB LYS A 452 68.865 7.134 57.821 1.00 29.87 2603 CG LYS A 452 68.343 7.423 59.227 1.00 34.10 2604 CD LYS A 452 69.048 6.450 60.162 1.00 38.10 2605 CE LYS A 452 68.830 6.729 61.640 1.00 40.92 2606 NZ LYS A 452 69.743 5.855 62.443 1.00 43.49 2607 N ASN A 453 68.621 6.628 54.808 1.00 22.30 2608 CA ASN A 453 69.323 6.230 53.583 1.00 22.25 2609 C ASN A 453 68.792 6.986 52.372 1.00 22.88 2610 O ASN A 453 68.213 6.412 51.448 1.00 20.10 2611 CB ASN A 453 69.185 4.732 53.390 1.00 22.17 2612 CG ASN A 453 69.885 3.894 54.438 1.00 22.47 2613 OD1 ASN A 453 69.207 3.368 55.345 1.00 26.98 2614 ND2 ASN A 453 71.168 3.715 54.360 1.00 18.00 2615 N LYS A 454 69.120 8.272 52.262 1.00 22.54 2616 CA LYS A 454 68.515 9.200 51.323 1.00 21.14 2617 C LYS A 454 68.895 8.936 49.881 1.00 20.78 2618 O LYS A 454 70.071 8.790 49.545 1.00 22.89 2619 CB LYS A 454 68.872 10.638 51.774 1.00 21.38 2620 CG LYS A 454 68.057 11.105 53.013 1.00 23.20 2621 CD LYS A 454 68.334 12.597 53.277 1.00 23.57 2622 CE LYS A 454 67.796 12.998 54.648 1.00 25.95 2623 NZ LYS A 454 66.341 12.839 54.758 1.00 26.08 2624 N GLY A 455 67.909 8.715 49.012 1.00 19.05 2625 CA GLY A 455 68.086 8.463 47.590 1.00 17.30 2626 C GLY A 455 68.350 7.013 47.242 1.00 17.20 2627 O GLY A 455 68.723 6.665 46.111 1.00 17.53 2628 N LYS A 456 68.270 6.123 48.226 1.00 15.28 2629 CA LYS A 456 68.659 4.734 48.032 1.00 16.32 2630 C LYS A 456 67.611 3.650 48.265 1.00 15.37 2631 O LYS A 456 66.603 3.951 48.904 1.00 15.63 2632 CB LYS A 456 69.787 4.424 49.040 1.00 18.28 2633 CG LYS A 456 70.918 5.434 49.114 1.00 18.06 2634 CD LYS A 456 72.081 4.992 48.231 1.00 19.93 2635 CE LYS A 456 73.093 6.121 48.121 1.00 20.50 2636 NZ LYS A 456 74.035 5.934 46.985 1.00 18.68 2637 N TYR A 457 67.870 2.454 47.758 1.00 14.15 2638 CA TYR A 457 66.986 1.341 47.981 1.00 13.53 2639 C TYR A 457 66.678 1.189 49.489 1.00 18.21 2640 O TYR A 457 65.487 1.011 49.788 1.00 13.29 2641 CB TYR A 457 67.490 −0.024 47.538 1.00 13.55 2642 CG TYR A 457 67.956 −0.142 46.075 1.00 14.83 2643 CD1 TYR A 457 69.241 −0.546 45.761 1.00 15.53 2644 CD2 TYR A 457 67.107 0.110 45.014 1.00 15.14 2645 CE1 TYR A 457 69.663 −0.645 44.409 1.00 15.97 2646 CE2 TYR A 457 67.460 0.018 43.665 1.00 15.67 2647 CZ TYR A 457 68.762 −0.369 43.408 1.00 16.86 2648 OH TYR A 457 69.165 −0.482 42.066 1.00 18.18 2649 N LEU A 458 67.603 1.255 50.450 1.00 17.70 2650 CA LEU A 458 67.335 0.919 51.869 1.00 18.01 2651 C LEU A 458 66.370 1.882 52.549 1.00 15.81 2652 O LEU A 458 65.802 1.650 53.669 1.00 14.97 2653 CB LEU A 458 68.678 0.861 52.699 1.00 17.40 2654 CG LEU A 458 69.584 −0.333 52.378 1.00 17.94 2655 CD1 LEU A 458 70.830 −0.312 53.282 1.00 20.17 2656 CD2 LEU A 458 68.866 −1.692 52.511 1.00 17.60 2657 N ALA A 459 66.132 3.071 51.984 1.00 15.65 2658 CA ALA A 459 65.167 4.005 52.608 1.00 16.80 2659 C ALA A 459 63.772 3.381 52.772 1.00 18.08 2660 O ALA A 459 63.016 3.656 53.718 1.00 15.52 2661 CB ALA A 459 65.103 5.260 51.750 1.00 14.58 2662 N PHE A 460 63.361 2.510 51.838 1.00 16.60 2663 CA PHE A 460 62.117 1.786 51.868 1.00 18.35 2664 C PHE A 460 62.017 0.683 52.942 1.00 19.16 2665 O PHE A 460 60.944 0.074 53.052 1.00 16.71 2666 CB PHE A 460 61.813 1.132 50.518 1.00 19.39 2667 CG PHE A 460 61.495 2.064 49.369 1.00 19.42 2668 CD1 PHE A 460 60.199 2.051 48.869 1.00 22.23 2669 CD2 PHE A 460 62.477 2.748 48.693 1.00 19.19 2670 CE1 PHE A 460 59.853 2.859 47.787 1.00 20.33 2671 CE2 PHE A 460 62.162 3.544 47.607 1.00 20.31 2672 CZ PHE A 460 60.847 3.590 47.141 1.00 20.55 2673 N THR A 461 63.086 0.410 53.727 1.00 17.62 2674 CA THR A 461 63.041 −0.515 54.824 1.00 17.58 2675 C THR A 461 62.842 0.254 56.179 1.00 17.98 2676 O THR A 461 62.824 −0.422 57.195 1.00 17.01 2677 CB THR A 461 64.340 −1.338 55.019 1.00 17.81 2678 OG1 THR A 461 65.418 −0.430 55.344 1.00 16.28 2679 CG2 THR A 461 64.706 −2.058 53.713 1.00 18.33 2680 N GLU A 462 62.820 1.569 56.197 1.00 17.91 2681 CA GLU A 462 62.881 2.254 57.509 1.00 18.73 2682 C GLU A 462 61.452 2.526 58.028 1.00 20.80 2683 O GLU A 462 60.651 3.247 57.389 1.00 17.17 2684 CB GLU A 462 63.597 3.584 57.237 1.00 19.94 2685 CG GLU A 462 65.032 3.372 56.651 1.00 20.13 2686 CD GLU A 462 65.759 4.695 56.580 1.00 21.29 2687 OE1 GLU A 462 65.461 5.602 57.401 1.00 22.06 2688 OE2 GLU A 462 66.629 4.885 55.702 1.00 20.07 2689 N HIS A 463 61.096 1.977 59.194 1.00 20.54 2690 CA HIS A 463 59.806 2.170 59.831 1.00 22.30 2691 C HIS A 463 59.778 3.350 60.778 1.00 22.71 2692 O HIS A 463 60.819 3.655 61.359 1.00 23.44 2693 CB HIS A 463 59.476 0.918 60.666 1.00 24.53 2694 CG HIS A 463 59.062 −0.209 59.775 1.00 26.84 2695 ND1 HIS A 463 59.954 −1.062 59.187 1.00 29.88 2696 CD2 HIS A 463 57.841 −0.611 59.362 1.00 28.11 2697 CE1 HIS A 463 59.315 −1.954 58.450 1.00 29.51 2698 NE2 HIS A 463 58.029 1.696 58.538 1.00 30.87 2699 N GLY A 464 58.637 3.962 61.066 1.00 23.85 2700 CA GLY A 464 58.547 5.049 62.031 1.00 22.89 2701 C GLY A 464 59.042 6.398 61.558 1.00 23.91 2702 O GLY A 464 59.256 7.293 62.406 1.00 21.28 2703 N THR A 465 59.227 6.617 60.250 1.00 21.74 2704 CA THR A 465 59.815 7.888 59.806 1.00 21.41 2705 C THR A 465 58.782 8.990 59.735 1.00 21.03 2706 O THR A 465 57.602 8.744 59.460 1.00 23.25 2707 CB THR A 465 60.563 7.738 58.467 1.00 22.09 2708 OG1 THR A 465 59.630 7.327 57.447 1.00 20.70 2709 CG2 THR A 465 61.643 6.667 58.699 1.00 21.72 2710 N LYS A 466 59.185 10.189 60.070 1.00 19.33 2711 CA LYS A 466 58.343 11.334 60.285 1.00 21.71 2712 C LYS A 466 58.905 12.549 59.557 1.00 21.36 2713 O LYS A 466 60.121 12.630 59.456 1.00 22.34 2714 CB LYS A 466 58.316 11.761 61.775 1.00 22.16 2715 CG LYS A 466 57.913 10.655 62.722 1.00 25.69 2716 CD LYS A 466 56.511 10.112 62.448 1.00 27.19 2717 CE LYS A 466 56.168 9.053 63.502 1.00 29.76 2718 NZ LYS A 466 54.932 8.298 63.127 1.00 29.77 2719 N GLY A 467 58.029 13.410 59.087 1.00 20.73 2720 CA GLY A 467 58.437 14.611 58.385 1.00 22.16 2721 C GLY A 467 57.855 15.833 59.110 1.00 23.57 2722 O GLY A 467 57.559 15.770 60.300 1.00 21.29 2723 N PRO A 468 57.742 16.944 58.387 1.00 24.04 2724 CA PRO A 468 57.264 18.188 58.952 1.00 24.86 2725 C PRO A 468 55.921 18.023 59.638 1.00 26.71 2726 O PRO A 468 55.032 17.290 59.223 1.00 24.09 2727 CB PRO A 468 57.252 19.135 57.761 1.00 24.51 2728 CG PRO A 468 58.442 18.647 56.967 1.00 24.08 2729 CD PRO A 468 58.260 17.127 57.004 1.00 23.34 2730 N ASP A 469 55.809 18.622 60.845 1.00 28.85 2731 CA ASP A 469 54.568 18.580 61.605 1.00 31.00 2732 C ASP A 469 54.190 17.167 62.012 1.00 29.54 2733 O ASP A 469 53.005 16.831 62.142 1.00 25.09 2734 CB ASP A 469 53.429 19.166 60.762 1.00 35.81 2735 CG ASP A 469 53.461 20.687 60.704 1.00 41.18 2736 OD1 ASP A 469 54.229 21.361 61.442 1.00 42.60 2737 OD2 ASP A 469 52.675 21.251 59.899 1.00 42.71 2738 N HIS A 470 55.216 16.314 62.194 1.00 27.09 2739 CA HIS A 470 54.991 14.943 62.567 1.00 29.90 2740 C HIS A 470 54.158 14.124 61.571 1.00 27.51 2741 O HIS A 470 53.713 13.036 61.986 1.00 25.40 2742 CB HIS A 470 54.351 14.933 63.968 1.00 35.53 2743 CG HIS A 470 54.966 13.762 64.690 1.00 41.88 2744 ND1 HIS A 470 54.293 12.781 65.341 1.00 44.60 2745 CD2 HIS A 470 56.338 13.553 64.868 1.00 44.13 2746 CE1 HIS A 470 55.239 11.999 65.896 1.00 45.27 2747 NE2 HIS A 470 56.472 12.438 65.630 1.00 45.71 2748 N VAL A 471 54.101 14.443 60.279 1.00 24.01 2749 CA VAL A 471 53.376 13.539 59.370 1.00 22.37 2750 C VAL A 471 54.211 12.254 59.214 1.00 21.98 2751 O VAL A 471 55.442 12.318 59.299 1.00 20.13 2752 CB VAL A 471 53.104 14.132 57.982 1.00 21.65 2753 CG1 VAL A 471 52.190 15.365 58.015 1.00 19.93 2754 CG2 VAL A 471 54.419 14.466 57.278 1.00 20.15 2755 N LYS A 472 53.542 11.139 58.935 1.00 19.69 2756 CA LYS A 472 54.244 9.876 58.649 1.00 18.37 2757 C LYS A 472 54.846 9.942 57.237 1.00 17.74 2758 O LYS A 472 54.211 10.506 56.321 1.00 17.56 2759 CB LYS A 472 53.212 8.750 58.700 1.00 21.16 2760 CG LYS A 472 52.495 8.535 60.043 1.00 20.15 2761 CD LYS A 472 51.529 7.341 59.924 1.00 21.24 2762 CE LYS A 472 51.192 6.810 61.317 1.00 25.17 2763 NZ LYS A 472 50.187 5.690 61.273 1.00 26.92 2764 N THR A 473 56.073 9.506 56.991 1.00 16.26 2765 CA THR A 473 56.650 9.508 55.639 1.00 17.04 2766 C THR A 473 57.096 8.108 55.226 1.00 16.39 2767 O THR A 473 56.881 7.201 56.041 1.00 14.08 2768 CB THR A 473 57.916 10.402 55.585 1.00 17.28 2769 OG1 THR A 473 58.862 9.885 56.543 1.00 17.62 2770 CG2 THR A 473 57.590 11.827 56.000 1.00 15.72 2771 N GLY A 474 57.706 7.921 54.044 1.00 15.36 2772 CA GLY A 474 58.229 6.588 53.720 1.00 15.08 2773 C GLY A 474 57.174 5.503 53.681 1.00 17.27 2774 O GLY A 474 55.985 5.776 53.434 1.00 15.09 2775 N ILE A 475 57.568 4.262 53.897 1.00 18.67 2776 CA ILE A 475 56.630 3.138 53.914 1.00 20.49 2777 C ILE A 475 55.474 3.256 54.907 1.00 19.29 2778 O ILE A 475 54.377 2.749 54.563 1.00 18.42 2779 CB ILE A 475 57.414 1.826 54.113 1.00 22.81 2780 CG1 ILE A 475 56.478 0.702 53.724 1.00 24.37 2781 CG2 ILE A 475 57.885 1.646 55.592 1.00 21.69 2782 CD1 ILE A 475 57.108 −0.682 53.618 1.00 28.52 2783 N ASP A 476 55.616 3.969 56.026 1.00 17.17 2784 CA ASP A 476 54.413 4.168 56.891 1.00 17.44 2785 C ASP A 476 53.387 5.060 56.185 1.00 16.48 2786 O ASP A 476 52.197 4.895 5.429 1.00 15.25 2787 CB ASP A 476 54.756 4.796 58.234 1.00 16.38 2788 CG ASP A 476 55.480 3.874 59.211 1.00 18.13 2789 OD1 ASP A 476 55.930 4.354 60.259 1.00 17.91 2790 OD2 ASP A 476 55.639 2.680 58.915 1.00 16.55 2791 N SER A 477 53.786 6.034 55.354 1.00 16.25 2792 CA SER A 477 52.848 6.880 54.629 1.00 16.55 2793 C SER A 477 52.108 6.065 53.549 1.00 18.34 2794 O SER A 477 50.912 6.237 53.283 1.00 19.12 2795 CB SER A 477 53.532 8.086 53.987 1.00 15.71 2796 OG SER A 477 52.610 8.857 53.192 1.00 17.49 2797 N LEU A 478 52.825 5.184 52.841 1.00 18.20 2798 CA LEU A 478 52.237 4.299 51.853 1.00 17.44 2799 C LEU A 478 51.154 3.403 52.475 1.00 19.05 2800 O LEU A 478 50.062 3.242 51.912 1.00 16.99 2801 CB LEU A 478 53.296 3.419 51.195 1.00 17.36 2802 CG LEU A 478 54.412 4.051 50.367 1.00 18.83 2803 CD1 LEU A 478 55.262 2.927 49.763 1.00 20.70 2804 CD2 LEU A 478 53.898 5.003 49.304 1.00 17.67 2805 N LYS A 479 51.418 2.843 53.647 1.00 20.29 2806 CA LYS A 479 50.448 2.085 54.413 1.00 23.91 2807 C LYS A 479 49.209 2.910 54.724 1.00 22.75 2808 O LYS A 479 48.056 2.535 54.473 1.00 23.72 2809 CB LYS A 479 51.049 1.642 55.759 1.00 27.33 2810 CG LYS A 479 50.226 0.539 56.358 1.00 32.76 2811 CD LYS A 479 50.636 −0.179 57.602 1.00 37.03 2812 CE LYS A 479 52.051 −0.291 58.088 1.00 40.23 2813 NZ LYS A 479 52.935 −1.004 57.114 1.00 42.37 2814 N GLU A 480 49.388 4.126 55.242 1.00 21.40 2815 CA GLU A 480 48.229 4.920 55.588 1.00 22.52 2816 C GLU A 480 47.449 5.378 54.364 1.00 19.27 2817 O GLU A 480 46.229 5.531 54.458 1.00 16.95 2818 CB GLU A 480 48.490 6.066 56.547 1.00 25.40 2819 CG GLU A 480 49.133 7.273 55.983 1.00 28.08 2820 CD GLU A 480 49.042 8.444 56.945 1.00 30.33 2821 OE1 GLU A 480 48.009 8.573 57.618 1.00 33.89 2822 OE2 GLU A 480 49.967 9.261 57.025 1.00 26.83 2823 N LEU A 481 48.091 5.482 53.220 1.00 19.95 2824 CA LEU A 481 47.406 5.891 51.984 1.00 16.96 2825 C LEU A 481 46.484 4.792 51.463 1.00 17.11 2826 O LEU A 481 45.404 5.121 50.925 1.00 15.46 2827 CB LEU A 481 48.502 6.240 50.976 1.00 17.20 2828 CG LEU A 481 48.070 6.823 49.640 1.00 17.62 2829 CD1 LEU A 481 47.221 8.098 49.831 1.00 18.14 2830 CD2 LEU A 481 49.273 7.277 48.811 1.00 14.35 2831 N GLY A 482 46.845 3.526 51.664 1.00 15.48 2832 CA GLY A 482 46.042 2.419 51.161 1.00 15.68 2833 C GLY A 482 46.507 1.767 49.851 1.00 16.09 2834 O GLY A 482 45.908 0.771 49.461 1.00 14.66 2835 N ILE A 483 47.483 2.333 49.124 1.00 15.13 2836 CA ILE A 483 47.942 1.737 47.849 1.00 15.05 2837 C ILE A 483 48.385 0.301 48.077 1.00 15.90 2838 O ILE A 483 48.723 −0.099 49.196 1.00 17.41 2839 CB ILE A 483 49.000 2.569 47.120 1.00 14.77 2840 CG1 ILE A 483 50.358 2.717 47.833 1.00 15.86 2841 CG2 ILE A 483 48.429 3.967 46.809 1.00 15.27 2842 CD1 ILE A 483 51.356 1.531 47.671 1.00 13.17 2843 N THR A 484 48.308 −0.555 47.050 1.00 15.28 2844 CA THR A 484 48.633 −1.952 47.213 1.00 15.28 2845 C THR A 484 49.933 −2.359 46.538 1.00 15.86 2846 O THR A 484 50.410 −3.469 46.796 1.00 13.72 2847 CB THR A 484 47.549 −2.863 46.532 1.00 16.48 2848 OG1 THR A 484 47.638 −2.693 45.102 1.00 16.43 2849 CG2 THR A 484 46.150 −2.505 47.003 1.00 16.06 2850 N THR A 485 50.443 −1.551 45.605 1.00 14.91 2851 CA THR A 485 51.595 −1.965 44.783 1.00 15.42 2852 C THR A 485 52.427 −0.757 44.384 1.00 15.53 2853 O THR A 485 51.863 0.244 43.919 1.00 15.10 2854 CB THR A 485 51.065 −2.655 43.513 1.00 15.83 2855 OG1 THR A 485 50.004 −3.584 43.802 1.00 16.38 2856 CG2 THR A 485 52.059 −3.489 42.695 1.00 16.14 2857 N VAL A 486 53.764 −0.790 44.555 1.00 14.94 2858 CA VAL A 486 54.652 0.297 44.134 1.00 12.74 2859 C VAL A 486 55.245 0.001 42.748 1.00 14.15 2860 O VAL A 486 55.788 −1.134 42.601 1.00 14.85 2861 CB VAL A 486 55.857 0.483 45.082 1.00 14.01 2862 CG1 VAL A 486 56.783 1.610 44.531 1.00 12.76 2863 CG2 VAL A 486 55.303 0.961 46.438 1.00 15.43 2864 N GLN A 487 55.159 0.899 41.798 1.00 12.39 2865 CA GLN A 487 55.823 0.699 40.507 1.00 13.69 2866 C GLN A 487 57.124 1.507 40.520 1.00 14.02 2867 O GLN A 487 57.008 2.717 40.530 1.00 15.37 2868 CB GLN A 487 54.975 1.132 39.304 1.00 14.53 2869 CG GLN A 487 55.555 0.810 37.899 1.00 14.85 2870 CD GLN A 487 54.658 1.489 36.844 1.00 15.25 2871 OE1 GLN A 487 53.542 0.999 36.600 1.00 12.63 2872 NE2 GLN A 487 55.086 2.600 36.263 1.00 14.69 2873 N LEU A 488 58.291 0.856 40.520 1.00 13.77 2874 CA LEU A 488 59.537 1.560 40.518 1.00 15.79 2875 C LEU A 488 60.035 1.987 39.152 1.00 15.05 2876 O LEU A 488 60.073 1.122 38.294 1.00 15.87 2877 CB LEU A 488 60.695 0.684 41.146 1.00 14.51 2878 CG LEU A 488 60.575 0.236 42.618 1.00 16.06 2879 CD1 LEU A 488 61.575 −0.885 42.971 1.00 15.85 2880 CD2 LEU A 488 60.742 1.336 43.642 1.00 11.74 2881 N GLN A 489 60.487 3.246 39.045 1.00 15.31 2882 CA GLN A 489 61.188 3.679 37.812 1.00 14.87 2883 C GLN A 489 62.425 2.807 37.665 1.00 14.33 2884 O GLN A 489 62.859 2.155 38.606 1.00 14.60 2885 CB GLN A 489 61.403 5.188 37.805 1.00 15.88 2886 CG GLN A 489 60.080 5.982 37.617 1.00 16.42 2887 CD GLN A 489 60.312 7.400 37.152 1.00 16.75 2888 OE1 GLN A 489 60.684 7.691 35.982 1.00 19.64 2889 NE2 GLN A 489 60.177 8.368 38.027 1.00 14.55 2890 N PRO A 490 63.045 2.689 36.494 1.00 14.20 2891 CA PRO A 490 64.089 1.703 36.225 1.00 13.53 2892 C PRO A 490 65.155 1.438 37.241 1.00 14.81 2893 O PRO A 490 65.895 2.388 37.605 1.00 15.34 2894 CB PRO A 490 64.707 2.269 34.906 1.00 13.82 2895 CG PRO A 490 63.479 2.776 34.197 1.00 15.17 2896 CD PRO A 490 62.691 3.502 35.299 1.00 11.82 2897 N VAL A 491 65.280 0.210 37.709 1.00 14.57 2898 CA VAL A 491 66.362 −0.156 38.655 1.00 16.33 2899 C VAL A 491 67.293 −1.160 37.970 1.00 17.32 2900 O VAL A 491 68.202 −1.714 38.584 1.00 17.98 2901 CB VAL A 491 65.792 −0.718 39.976 1.00 35.46 2902 CG1 VAL A 491 64.974 0.369 40.708 1.00 13.55 2903 CG2 VAL A 491 64.915 −1.944 39.688 1.00 14.62 2904 N GLU A 492 67.092 −1.504 36.697 1.00 18.44 2905 CA GLU A 492 68.031 −2.245 35.863 1.00 16.40 2906 C GLU A 492 69.156 −1.271 35.451 1.00 17.63 2907 O GLU A 492 68.937 −0.141 34.964 1.00 15.32 2908 CB GLU A 492 67.459 −2.927 34.598 1.00 15.59 2909 CG GLU A 492 66.412 −4.003 34.981 1.00 16.27 2910 CD GLU A 492 65.731 −4.713 33.824 1.00 16.24 2911 OE1 GLU A 492 65.079 −5.765 33.984 1.00 15.93 2912 OE2 GLU A 492 65.871 −4.235 32.678 1.00 16.98 2913 N GLU A 493 70.400 −1.716 35.653 1.00 17.89 2914 CA GLU A 493 71.592 −0.901 35.413 1.00 18.19 2915 C GLU A 493 71.592 −0.092 34.107 1.00 17.67 2916 O GLU A 493 71.579 −0.640 33.012 1.00 15.24 2917 CB GLU A 493 72.869 −1.773 35.447 1.00 18.34 2918 CG GLU A 493 74.173 −1.020 35.230 1.00 18.92 2919 CD GLU A 493 74.742 −0.344 36.455 1.00 19.23 2920 OE1 GLU A 493 75.796 0.334 36.325 1.00 17.41 2921 OE2 GLU A 493 74.095 −0.479 37.541 1.00 19.62 2922 N PHE A 494 71.755 1.230 34.238 1.00 15.08 2923 CA PHE A 494 71.716 2.064 33.051 1.00 17.22 2924 C PHE A 494 73.040 2.834 32.904 1.00 17.93 2925 O PHE A 494 73.846 2.871 33.840 1.00 17.61 2926 CB PHE A 494 70.494 2.985 33.079 1.00 15.05 2927 CG PHE A 494 70.209 3.732 34.347 1.00 13.69 2928 CD1 PHE A 494 69.309 3.238 35.283 1.00 13.97 2929 CD2 PHE A 494 70.814 4.964 34.603 1.00 14.09 2930 CE1 PHE A 494 69.008 3.927 36.442 1.00 13.34 2931 CE2 PHE A 494 70.548 5.662 35.766 1.00 13.82 2932 CZ PHE A 494 69.650 5.128 36.706 1.00 14.68 2933 N ASN A 495 73.262 3.489 31.758 1.00 17.56 2934 CA ASN A 495 74.549 4.074 31.443 1.00 19.21 2935 C ASN A 495 74.759 5.505 31.926 1.00 18.67 2936 O ASN A 495 75.915 5.887 32.059 1.00 17.87 2937 CB ASN A 495 74.850 4.084 29.931 1.00 17.20 2938 CG ASN A 495 76.266 4.473 29.570 1.00 20.20 2939 OD1 ASN A 495 77.257 3.802 29.891 1.00 18.77 2940 ND2 ASN A 495 76.482 5.618 28.938 1.00 19.57 2941 N SER A 496 73.715 6.299 32.041 1.00 17.59 2942 CA SER A 496 73.827 7.723 32.297 1.00 17.54 2943 C SER A 496 74.342 8.127 33.652 1.00 18.68 2944 O SER A 496 74.638 9.331 33.798 1.00 18.94 2945 CB SER A 496 72.487 8.433 32.001 1.00 19.07 2946 OG SER A 496 71.377 7.889 32.711 1.00 17.68 2947 N ILE A 497 74.441 7.273 34.670 1.00 16.74 2948 CA ILE A 497 75.071 7.777 35.908 1.00 17.05 2949 C ILE A 497 76.434 7.104 36.029 1.00 17.86 2950 O ILE A 497 76.528 5.880 35.928 1.00 16.60 2951 CB ILE A 497 74.203 7.473 37.156 1.00 18.85 2952 CG1 ILE A 497 72.950 8.366 37.145 1.00 18.39 2953 CG2 ILE A 497 75.033 7.586 38.435 1.00 16.11 2954 CD1 ILE A 497 71.845 8.001 38.145 1.00 18.90 2955 N ASP A 498 77.478 7.888 36.227 1.00 18.34 2956 CA ASP A 498 78.806 7.346 36.522 1.00 19.14 2957 C ASP A 498 78.770 6.898 37.971 1.00 17.01 2958 O ASP A 498 78.609 7.762 38.858 1.00 15.12 2959 CB ASP A 498 79.861 8.458 36.364 1.00 21.90 2960 CG ASP A 498 81.295 8.069 36.759 1.00 24.10 2961 OD1 ASP A 498 82.155 8.832 36.229 1.00 23.49 2962 OD2 ASP A 498 81.615 7.096 37.480 1.00 19.87 2963 N GLU A 499 79.011 5.646 38.280 1.00 16.55 2964 CA GLU A 499 78.977 5.108 39.632 1.00 19.92 2965 C GLU A 499 79.988 5.691 40.614 1.00 21.17 2966 O GLU A 499 79.775 5.543 41.836 1.00 20.23 2967 CB GLU A 499 79.090 3.565 39.610 1.00 18.52 2968 CG GLU A 499 77.783 3.044 38.948 1.00 17.11 2969 CD GLU A 499 77.715 1.561 38.901 1.00 19.30 2970 OE1 GLU A 499 78.782 0.866 38.946 1.00 18.97 2971 OE2 GLU A 499 76.609 0.973 38.775 1.00 18.01 2972 N THR A 500 81.008 4.404 40.126 1.00 20.80 2973 CA THR A 500 81.940 7.053 41.057 1.00 23.34 2974 C THR A 500 81.372 8.400 41.497 1.00 24.20 2975 O THR A 500 82.015 9.077 42.287 1.00 24.37 2976 CB THR A 500 83.342 7.317 40.473 1.00 21.92 2977 OG1 THR A 500 83.230 8.244 39.379 1.00 20.76 2978 CG2 THR A 500 84.023 6.044 39.986 1.00 22.58 2979 N GLN A 501 80.313 8.895 40.895 1.00 26.63 2980 CA GLN A 501 79.580 10.111 41.217 1.00 29.35 2981 C GLN A 501 78.081 9.780 41.293 1.00 29.18 2982 O GLN A 501 77.286 10.114 40.421 1.00 28.10 2983 CB GLN A 501 79.695 11.145 40.089 1.00 32.33 2984 CG GLN A 501 81.113 11.471 39.637 1.00 36.70 2985 CD GLN A 501 81.850 12.239 40.710 1.00 41.32 2986 OE1 GLN A 501 81.235 12.619 41.723 1.00 43.52 2987 NE2 GLN A 501 83.153 12.497 40.515 1.00 44.21 2988 N PRO A 502 77.652 9.030 42.297 1.00 29.53 2989 CA PRO A 502 76.292 8.507 42.359 1.00 28.54 2990 C PRO A 502 75.175 9.471 42.670 1.00 28.87 2991 O PRO A 502 74.004 9.050 42.701 1.00 30.15 2992 CB PRO A 502 76.406 7.392 43.399 1.00 26.18 2993 CG PRO A 502 77.510 7.853 44.309 1.00 27.23 2994 CD PRO A 502 78.477 8.622 43.471 1.00 27.08 2995 N ASP A 503 75.432 10.751 42.881 1.00 28.94 2996 CA ASP A 503 74.380 11.709 43.179 1.00 29.84 2997 C ASP A 503 73.930 12.521 41.976 1.00 28.92 2998 O ASP A 503 73.125 13.446 42.132 1.00 30.62 2999 CB ASP A 503 74.783 12.642 44.344 1.00 29.97 3000 CG ASP A 503 74.845 11.877 45.654 1.00 31.52 3001 OD1 ASP A 503 74.016 10.975 45.912 1.00 29.14 3002 OD2 ASP A 503 75.783 12.160 46.439 1.00 33.43 3003 N THR A 504 74.384 12.204 40.790 1.00 28.14 3004 CA THR A 504 73.894 12.795 39.547 1.00 28.02 3005 C THR A 504 72.464 12.303 39.332 1.00 25.44 3006 O THR A 504 72.090 11.307 39.988 1.00 26.41 3007 CB THR A 504 74.817 12.287 38.421 1.00 30.26 3008 OG1 THR A 504 74.365 12.697 37.137 1.00 34.86 3009 CG2 THR A 504 74.853 10.784 38.452 1.00 32.35 3010 N TYR A 505 71.617 12.976 38.574 1.00 22.48 3011 CA TYR A 505 70.198 12.564 38.498 1.00 20.51 3012 C TYR A 505 69.839 11.991 37.135 1.00 20.40 3013 O TYR A 505 70.037 12.679 36.103 1.00 19.81 3014 CB TYR A 505 69.281 13.777 38.795 1.00 19.30 3015 CG TYR A 505 67.814 13.347 38.862 1.00 19.19 3016 CD1 TYR A 505 67.241 13.027 40.115 1.00 17.54 3017 CD2 TYR A 505 67.023 13.226 37.730 1.00 16.46 3018 CE1 TYR A 505 65.931 12.559 40.199 1.00 16.03 3019 CE2 TYR A 505 65.697 12.777 37.831 1.00 16.62 3020 CZ TYR A 505 65.163 12.442 39.058 1.00 17.37 3021 OH TYR A 505 63.859 11.975 39.132 1.00 16.33 3022 N ASN A 506 69.117 10.864 37.112 1.00 19.02 3023 CA ASN A 506 68.525 10.394 35.854 1.00 17.54 3024 C ASN A 506 67.354 9.433 36.132 1.00 16.94 3025 O ASN A 506 67.448 8.585 37.023 1.00 15.04 3026 CB ASN A 506 69.538 9.697 34.935 1.00 17.11 3027 CG ASN A 506 69.102 9.692 33.481 1.00 19.56 3028 OD1 ASN A 506 68.263 8.880 33.019 1.00 18.08 3029 ND2 ASN A 506 69.679 10.641 32.729 1.00 18.09 3030 N TRP A 507 66.363 9.479 35.216 1.00 14.78 3031 CA TRP A 507 65.263 8.515 35.282 1.00 14.79 3032 C TRP A 507 65.716 7.096 34.995 1.00 14.58 3033 O TRP A 507 65.101 6.151 35.466 1.00 12.62 3034 CB TRP A 507 64.189 8.879 34.236 1.00 13.89 3035 CG TRP A 507 63.208 9.944 34.647 1.00 13.96 3036 CD1 TRP A 507 63.021 10.504 35.878 1.00 13.86 3037 CD2 TRP A 507 62.268 10.598 33.765 1.00 13.76 3038 NE1 TRP A 507 62.035 11.509 35.797 1.00 14.63 3039 CE2 TRP A 507 61.572 11.557 34.520 1.00 14.09 3040 CE3 TRP A 507 62.006 10.488 32.396 1.00 14.36 3041 CZ2 TRP A 507 60.623 12.410 33.943 1.00 15.35 3042 CZ3 TRP A 507 61.039 11.314 31.837 1.00 16.79 3043 CH2 TRP A 507 60.359 12.283 32.620 1.00 14.29 3044 N GLY A 508 66.779 6.933 34.176 1.00 14.06 3045 CA GLY A 508 67.280 5.621 33.845 1.00 14.97 3046 C GLY A 508 66.688 4.906 32.664 1.00 14.99 3047 O GLY A 508 66.794 3.661 32.610 1.00 13.65 3048 N TYR A 509 66.161 5.623 31.664 1.00 15.66 3049 CA TYR A 509 65.673 5.037 30.419 1.00 16.40 3050 C TYR A 509 66.771 4.746 29.389 1.00 16.91 3051 O TYR A 509 66.436 4.451 28.241 1.00 16.03 3052 CB TYR A 509 64.471 5.812 29.758 1.00 14.79 3053 CG TYR A 509 63.288 5.731 30.729 1.00 17.63 3054 CD1 TYR A 509 62.469 4.608 30.816 1.00 15.29 3055 CD2 TYR A 509 63.037 6.779 31.616 1.00 17.85 3056 CE1 TYR A 509 61.434 4.549 31.726 1.00 14.88 3057 CE2 TYR A 509 62.012 6.735 32.540 1.00 17.47 3058 CZ TYR A 509 61.210 5.585 32.587 1.00 18.26 3059 OH TYR A 509 60.204 5.532 33.541 1.00 18.82 3060 N ASP A 510 68.021 4.495 29.735 1.00 16.31 3061 CA ASP A 510 69.142 4.129 28.870 1.00 18.35 3062 C ASP A 510 69.891 2.912 29.392 1.00 17.34 3063 O ASP A 510 71.041 2.945 29.873 1.00 20.99 3064 CB ASP A 510 70.120 5.322 28.723 1.00 19.25 3065 CG ASP A 510 70.746 5.804 30.000 1.00 21.01 3066 OD1 ASP A 510 70.057 5.942 31.032 1.00 21.87 3067 OD2 ASP A 510 71.991 6.068 30.056 1.00 23.52 3068 N PRO A 511 69.294 1.752 29.370 1.00 16.56 3069 CA PRO A 511 69.789 0.507 29.915 1.00 17.26 3070 C PRO A 511 71.112 0.019 29.272 1.00 17.06 3071 O PRO A 511 71.327 0.259 28.077 1.00 16.16 3072 CB PRO A 511 68.730 −0.564 29.675 1.00 16.53 3073 CG PRO A 511 67.898 −0.001 28.531 1.00 17.61 3074 CD PRO A 511 67.914 1.498 28.752 1.00 17.12 3075 N ARG A 512 71.925 −0.624 30.102 1.00 16.69 3076 CA ARG A 512 73.212 −1.174 29.634 1.00 16.56 3077 C ARG A 512 73.392 −2.618 30.065 1.00 16.11 3078 O ARG A 512 73.824 −3.472 29.278 1.00 16.43 3079 CB ARG A 512 74.394 −0.275 30.088 1.00 18.15 3080 CG ARG A 512 75.778 −0.703 29.616 1.00 18.63 3081 CD ARG A 512 76.929 0.127 30.219 1.00 19.47 3082 NE ARG A 512 77.011 −0.045 31.687 1.00 20.90 3083 CZ ARG A 512 77.354 0.937 32.563 1.00 20.85 3084 NH1 ARG A 512 77.328 0.708 33.877 1.00 20.82 3085 NH2 ARG A 512 77.653 2.184 32.233 1.00 19.17 3086 N ASN A 513 73.175 −2.970 31.326 1.00 15.21 3087 CA ASN A 513 73.323 −4.307 31.896 1.00 14.14 3088 C ASN A 513 71.957 −4.696 32.471 1.00 15.83 3089 O ASN A 513 71.562 −4.414 33.623 1.00 14.75 3090 CB ASN A 513 74.425 −4.304 32.991 1.00 13.68 3091 CG ASN A 513 75.722 −3.670 32.503 1.00 15.65 3092 OD1 ASN A 513 75.960 −2.463 32.702 1.00 13.93 3093 ND2 ASN A 513 76.592 −4.443 31.817 1.00 13.93 3094 N TYR A 514 71.137 −5.398 31.687 1.00 16.49 3095 CA TYR A 514 69.742 −5.666 32.068 1.00 17.77 3096 C TYR A 514 69.496 −6.572 33.280 1.00 18.89 3097 O TYR A 514 68.398 −6.564 33.865 1.00 16.26 3098 CB TYR A 514 69.017 −6.266 30.861 1.00 18.16 3099 CG TYR A 514 68.726 −5.341 29.689 1.00 18.97 3100 CD1 TYR A 514 67.565 −4.560 29.672 1.00 18.42 3101 CD2 TYR A 514 69.604 −5.279 28.597 1.00 19.59 3102 CE1 TYR A 514 67.289 −3.734 28.595 1.00 18.29 3103 CE2 TYR A 514 69.328 −4.444 27.514 1.00 19.38 3104 CZ TYR A 514 68.167 −3.696 27.521 1.00 19.34 3105 OH TYR A 514 67.857 −2.887 26.450 1.00 22.29 3106 N ASN A 515 70.493 −7.389 33.643 1.00 17.63 3107 CA ASN A 515 70.280 −8.339 34.745 1.00 17.34 3108 C ASN A 515 70.978 −7.906 36.018 1.00 17.54 3109 O ASN A 515 71.187 −8.752 36.913 1.00 18.12 3110 CB ASN A 515 70.786 −9.703 34.185 1.00 16.85 3111 CG ASN A 515 69.974 −10.095 32.944 1.00 18.64 3112 OD1 ASN A 515 70.465 −10.350 31.826 1.00 21.03 3113 ND2 ASN A 515 68.680 −10.119 33.147 1.00 11.82 3114 N VAL A 516 71.402 −6.661 36.141 1.00 14.31 3115 CA VAL A 516 72.083 −6.138 37.344 1.00 15.74 3116 C VAL A 516 71.301 −4.960 37.911 1.00 16.74 3117 O VAL A 516 70.892 −4.053 37.176 1.00 16.35 3118 CB VAL A 516 73.478 −5.606 36.838 1.00 16.38 3119 CG1 VAL A 516 74.289 −4.915 37.924 1.00 15.90 3120 CG2 VAL A 516 74.293 −6.720 36.163 1.00 15.48 3121 N PRO A 517 71.121 −4.832 39.223 1.00 17.59 3122 CA PRO A 517 70.522 −3.663 39.846 1.00 15.46 3123 C PRO A 517 71.370 −2.408 39.664 1.00 16.15 3124 O PRO A 517 72.601 −2.451 39.870 1.00 17.59 3125 CB PRO A 517 70.481 −4.030 41.330 1.00 16.03 3126 CG PRO A 517 70.630 −5.532 41.363 1.00 16.94 3127 CD PRO A 517 71.656 −5.777 40.261 1.00 15.72 3128 N GLU A 518 70.756 −1.245 39.475 1.00 13.80 3129 CA GLU A 518 71.457 0.025 39.340 1.00 15.14 3130 C GLU A 518 72.366 0.288 40.567 1.00 15.73 3131 O GLU A 518 71.844 0.352 41.694 1.00 14.71 3132 CB GLU A 518 70.444 1.149 39.065 1.00 14.95 3133 CG GLU A 518 71.065 2.558 39.118 1.00 15.19 3134 CD GLU A 518 72.139 2.790 38.080 1.00 17.66 3135 OE1 GLU A 518 72.129 2.189 36.974 1.00 16.65 3136 OE2 GLU A 518 73.093 3.591 38.350 1.00 17.95 3137 N GLY A 519 73.671 0.589 40.305 1.00 15.19 3138 CA GLY A 519 74.567 0.786 41.499 1.00 15.74 3139 C GLY A 519 74.412 2.112 42.221 1.00 15.83 3140 O GLY A 519 74.575 2.196 43.455 1.00 14.13 3141 N ALA A 520 73.905 3.163 41.577 1.00 16.04 3142 CA ALA A 520 73.780 4.471 42.239 1.00 18.29 3143 C ALA A 520 72.771 4.499 43.381 1.00 18.95 3144 O ALA A 520 72.856 5.422 44.196 1.00 16.80 3145 CB ALA A 520 73.427 5.513 41.206 1.00 18.41 3146 N TYR A 521 71.811 3.561 43.410 1.00 17.07 3147 CA TYR A 521 70.819 3.494 44.486 1.00 16.73 3148 C TYR A 521 71.260 2.579 45.612 1.00 17.27 3149 O TYR A 521 70.528 2.470 46.610 1.00 17.61 3150 CB TYR A 521 69.446 3.021 43.941 1.00 17.24 3151 CG TYR A 521 68.942 3.859 42.764 1.00 15.38 3152 CD1 TYR A 521 69.117 5.247 42.743 1.00 15.18 3153 CD2 TYR A 521 68.284 3.264 41.724 1.00 15.31 3154 CE1 TYR A 521 68.738 6.002 41.655 1.00 16.88 3155 CE2 TYR A 521 67.798 4.003 40.641 1.00 16.48 3156 CZ TYR A 521 68.057 5.367 40.617 1.00 17.62 3157 OH TYR A 521 67.606 6.097 39.531 1.00 19.26 3158 N ALA A 522 72.417 1.907 45.435 1.00 17.17 3159 CA ALA A 522 72.945 1.042 46.518 1.00 15.89 3160 C ALA A 522 73.921 1.876 47.348 1.00 15.60 3161 O ALA A 522 74.342 2.981 46.946 1.00 17.19 3162 CB ALA A 522 73.659 −0.164 45.905 1.00 13.85 3163 N THR A 523 74.102 1.561 48.625 1.00 15.78 3164 CA THR A 523 75.072 2.230 49.489 1.00 17.82 3165 C THR A 523 76.470 1.956 48.944 1.00 18.92 3166 O THR A 523 77.211 2.947 49.304 1.00 17.26 3167 CB THR A 523 74.948 1.890 50.976 1.00 17.94 3168 OG1 THR A 523 75.385 0.524 51.116 1.00 17.69 3169 CG2 THR A 523 73.506 2.011 51.516 1.00 16.78 3170 N THR A 524 76.940 1.218 48.019 1.00 16.59 3171 CA THR A 524 78.214 1.239 47.375 1.00 17.47 3172 C THR A 524 77.987 0.549 46.014 1.00 15.97 3173 O THR A 524 77.245 −0.434 46.035 1.00 15.00 3174 CB THR A 524 79.381 0.537 48.089 1.00 16.77 3175 OG1 THR A 524 80.598 0.447 47.315 1.00 18.09 3176 CG2 THR A 524 79.009 −0.895 48.485 1.00 17.48 3177 N PRO A 525 78.671 0.941 44.975 1.00 16.83 3178 CA PRO A 525 78.667 0.231 43.696 1.00 16.43 3179 C PRO A 525 79.532 −1.019 43.697 1.00 17.20 3180 O PRO A 525 79.479 −1.868 42.773 1.00 16.05 3181 CB PRO A 525 79.261 1.241 42.734 1.00 17.75 3182 CG PRO A 525 80.236 2.061 43.551 1.00 17.07 3183 CD PRO A 525 79.581 2.153 44.935 1.00 16.46 3184 N GLU A 526 80.334 −1.296 44.754 1.00 17.68 3185 CA GLU A 526 81.242 −2.413 44.797 1.00 15.57 3186 C GLU A 526 80.552 −3.755 45.025 1.00 18.65 3187 O GLU A 526 79.678 −3.828 45.910 1.00 17.57 3188 CB GLU A 526 82.241 −2.286 45.993 1.00 18.74 3189 CG GLU A 526 83.196 −1.098 45.920 1.00 17.93 3190 CD GLU A 526 84.240 −1.354 44.831 1.00 20.14 3191 OE1 GLU A 526 84.455 −2.518 44.447 1.00 18.35 3192 OE2 GLU A 526 84.830 −0.361 44.367 1.00 20.55 3193 N GLY A 527 80.932 −4.816 44.303 1.00 16.41 3194 CA GLY A 527 80.349 −6.100 44.587 1.00 18.62 3195 C GLY A 527 78.868 −6.310 44.654 1.00 19.21 3196 O GLY A 527 78.114 −5.715 43.903 1.00 19.86 3197 N THR A 528 78.364 −7.119 45.605 1.00 20.27 3198 CA THR A 528 76.950 −7.510 45.574 1.00 18.39 3199 C THR A 528 76.092 −6.707 46.515 1.00 19.42 3200 O THR A 528 74.938 −7.063 46.774 1.00 18.50 3201 CB THR A 528 76.855 −9.024 45.904 1.00 18.15 3202 OG1 THR A 528 77.414 −9.233 47.211 1.00 20.44 3203 CG2 THR A 528 77.688 −9.855 44.941 1.00 17.77 3204 N ALA A 529 76.662 −5.642 47.063 1.00 18.16 3205 CA ALA A 529 75.933 −4.712 47.906 1.00 18.05 3206 C ALA A 529 74.630 −4.330 47.203 1.00 18.52 3207 O ALA A 529 73.580 −4.348 47.859 1.00 16.31 3208 CB ALA A 529 76.703 −3.413 48.157 1.00 18.09 3209 N ARG A 530 74.624 −4.063 45.907 1.00 17.37 3210 CA ARG A 530 73.422 −3.669 45.184 1.00 16.22 3211 C ARG A 530 72.334 −4.739 45.116 1.00 16.28 3212 O ARG A 530 71.148 −4.377 45.045 1.00 15.45 3213 CB ARG A 530 73.783 −3.225 43.762 1.00 15.05 3214 CG ARG A 530 74.440 −4.346 42.940 1.00 16.74 3215 CD ARG A 530 74.961 −3.751 41.630 1.00 14.90 3216 NE ARG A 530 76.197 −2.937 41.763 1.00 15.63 3217 CZ ARG A 530 76.515 −2.064 40.802 1.00 15.30 3218 NH1 ARG A 530 77.670 −1.407 40.853 1.00 17.75 3219 NH2 ARG A 530 75.706 −1.836 39.773 1.00 12.09 3220 N ILE A 531 72.700 −6.005 45.108 1.00 14.54 3221 CA ILE A 531 71.804 −7.113 45.021 1.00 17.37 3222 C ILE A 531 71.001 −7.347 46.318 1.00 18.65 3223 O ILE A 531 69.754 −7.487 46.311 1.00 14.76 3224 CB ILE A 531 72.556 −8.391 44.601 1.00 17.38 3225 CG1 ILE A 531 73.146 −8.298 43.182 1.00 17.59 3226 CG2 ILE A 531 71.624 −9.601 44.601 1.00 16.93 3227 CD1 ILE A 531 73.965 −9.553 42.804 1.00 16.77 3228 N THR A 532 71.717 −7.408 47.426 1.00 16.30 3229 CA THR A 532 71.120 −7.596 48.745 1.00 17.14 3230 C THR A 532 70.203 −6.408 49.093 1.00 16.96 3231 O THR A 532 69.122 −6.670 49.634 1.00 17.94 3232 CB THR A 532 72.202 −7.696 49.838 1.00 18.30 3233 OG1 THR A 532 73.048 −8.840 49.519 1.00 17.90 3234 CG2 THR A 532 71.578 −7.989 51.205 1.00 15.71 3235 N GLU A 533 70.608 −5.180 48.808 1.00 13.67 3236 CA GLU A 533 69.821 −3.993 49.110 1.00 15.12 3237 C GLU A 533 68.532 −3.891 48.317 1.00 16.63 3238 O GLU A 533 67.551 −3.400 48.903 1.00 14.08 3239 CB GLU A 533 70.707 −2.740 49.008 1.00 16.01 3240 CG GLU A 533 71.682 −2.653 50.183 1.00 17.57 3241 CD GLU A 533 72.716 −1.580 50.093 1.00 19.20 3242 OE1 GLU A 533 73.811 −1.717 50.714 1.00 21.48 3243 OE2 GLU A 533 72.475 −0.536 49.428 1.00 20.43 3244 N LEU A 534 68.465 −4.294 47.052 1.00 14.75 3245 CA LEU A 534 67.179 −4.230 46.320 1.00 14.76 3246 C LEU A 534 66.255 −5.331 46.838 1.00 13.97 3247 O LEU A 534 65.040 −5.162 46.998 1.00 13.22 3248 CB LEU A 534 67.451 −4.277 44.804 1.00 11.25 3249 CG LEU A 534 66.205 −4.408 43.904 1.00 13.31 3250 CD1 LEU A 534 65.165 −3.291 44.168 1.00 10.17 3251 CD2 LEU A 534 66.721 −4.308 42.454 1.00 10.59 3252 N LYS A 535 66.805 −6.516 47.087 1.00 13.87 3253 CA LYS A 535 66.086 −7.618 47.715 1.00 15.88 3254 C LYS A 535 65.530 −7.196 49.082 1.00 16.79 3255 O LYS A 535 64.377 −7.547 49.376 1.00 17.52 3256 CB LYS A 535 66.887 −8.917 47.860 1.00 15.40 3257 CG LYS A 535 67.402 −9.601 46.617 1.00 18.60 3258 CD LYS A 535 68.119 −10.918 46.903 1.00 17.82 3259 CE LYS A 535 68.558 −11.541 45.575 1.00 18.33 3260 NZ LYS A 535 69.546 −12.644 45.766 1.00 16.36 3261 N GLN A 536 66.207 −6.389 49.915 1.00 16.15 3262 CA GLN A 536 65.663 −5.931 51.188 1.00 17.43 3263 C GLN A 536 64.484 −4.948 51.011 1.00 15.85 3264 O GLN A 536 63.556 −4.932 51.829 1.00 13.29 3265 CB GLN A 536 66.735 −5.260 52.068 1.00 16.73 3266 CG GLN A 536 67.783 −6.230 52.583 1.00 20.31 3267 CD GLN A 536 68.982 −5.556 53.221 1.00 22.94 3268 OE1 GLN A 536 69.836 −4.925 52.614 1.00 21.17 3269 NE2 GLN A 536 69.036 −5.681 54.536 1.00 25.61 3270 N LEU A 537 64.505 −4.105 49.992 1.00 16.38 3271 CA LEU A 537 63.425 −3.174 49.650 1.00 16.60 3272 C LEU A 537 62.179 −4.051 49.336 1.00 17.04 3273 O LEU A 537 61.080 −3.702 49.797 1.00 16.16 3274 CB LEU A 537 63.756 −2.314 48.435 1.00 17.59 3275 CG LEU A 537 62.757 −1.314 47.829 1.00 15.05 3276 CD1 LEU A 537 63.348 −0.200 46.975 1.00 16.00 3277 CD2 LEU A 537 61.771 −2.134 46.970 1.00 15.65 3278 N ILE A 538 62.361 −5.013 48.468 1.00 16.09 3279 CA ILE A 538 61.288 −5.922 48.067 1.00 16.51 3280 C ILE A 538 60.701 −6.677 49.245 1.00 17.89 3281 O ILE A 538 59.479 −6.811 49.400 1.00 16.47 3282 CB ILE A 538 61.777 6.836 46.920 1.00 16.94 3283 CG1 ILE A 538 62.083 −5.982 45.686 1.00 14.36 3284 CG2 ILE A 538 60.667 −7.886 46.675 1.00 17.13 3285 CD1 ILE A 538 62.805 −6.628 44.509 1.00 13.95 3286 N GLN A 539 61.538 −7.186 50.141 1.00 16.57 3287 CA GLN A 539 61.128 −7.943 51.314 1.00 17.53 3288 C GLN A 539 60.345 −7.077 52.312 1.00 18.11 3289 O GLN A 539 59.366 −7.553 52.893 1.00 17.99 3290 CB GLN A 539 62.351 −8.523 52.027 1.00 19.31 3291 CG GLN A 539 62.149 −9.256 53.324 1.00 19.71 3292 CD GLN A 539 63.417 −9.837 53.936 1.00 20.54 3293 OE1 GLN A 539 64.431 −9.149 54.033 1.00 22.88 3294 NE2 GLN A 539 63.404 −11.074 54.356 1.00 19.77 3295 N SER A 540 60.765 −5.844 52.489 1.00 18.42 3296 CA SER A 540 60.102 −4.916 53.403 1.00 20.34 3297 C SER A 540 58.723 −4.480 52.906 1.00 20.30 3298 O SER A 540 57.763 −4.529 53.714 1.00 16.87 3299 CB SER A 540 61.125 −3.801 53.586 1.00 21.39 3300 OG SER A 540 60.542 −2.651 54.113 1.00 26.78 3301 N LEU A 541 58.502 −4.242 51.613 1.00 17.30 3302 CA LEU A 541 57.127 −3.909 51.140 1.00 18.58 3303 C LEU A 541 56.231 −5.132 51.270 1.00 18.04 3304 O LEU A 541 55.047 −5.034 51.690 1.00 17.70 3305 CB LEU A 541 57.128 −3.311 49.731 1.00 19.55 3306 CG LEU A 541 57.908 −2.022 49.522 1.00 20.99 3307 CD1 LEU A 541 58.100 −1.486 48.104 1.00 20.76 3308 CD2 LEU A 541 57.190 −0.836 50.210 1.00 21.46 3309 N HIS A 542 56.739 −6.322 50.902 1.00 15.72 3310 CA HIS A 542 55.993 −7.545 50.990 1.00 17.12 3311 C HIS A 542 55.499 −7.790 52.421 1.00 20.37 3312 O HIS A 542 54.326 −8.187 52.598 1.00 17.99 3313 CB HIS A 542 56.747 −8.783 50.476 1.00 17.02 3314 CG HIS A 542 56.882 −8.831 48.975 1.00 16.64 3315 ND1 HIS A 542 57.700 −9.780 48.377 1.00 15.29 3316 CD2 HIS A 542 56.349 −8.154 47.933 1.00 14.04 3317 CE1 HIS A 542 57.670 −9.669 47.055 1.00 15.74 3318 NE2 HIS A 542 56.848 −8.690 46.754 1.00 14.08 3319 N GLN A 543 56.340 −7.489 53.425 1.00 19.61 3320 CA GLN A 543 55.955 −7.702 54.817 1.00 22.30 3321 C GLN A 543 54.786 −6.794 55.164 1.00 22.43 3322 O GLN A 543 54.023 −7.124 56.093 1.00 20.41 3323 CB GLN A 543 57.132 −7.462 55.797 1.00 23.32 3324 CG GLN A 543 58.247 −8.469 55.718 1.00 26.39 3325 CD GLN A 543 59.583 −8.082 56.334 1.00 29.94 3326 OE1 GLN A 543 60.499 −8.911 56.516 1.00 29.73 3327 NE2 GLN A 543 59.764 −6.816 56.705 1.00 28.77 3328 N GLN A 544 54.621 −5.649 54.503 1.00 21.34 3329 CA GLN A 544 53.444 −4.814 54.771 1.00 24.96 3330 C GLN A 544 52.339 −5.016 53.751 1.00 23.83 3331 O GLN A 544 51.495 −4.154 53.42 1.00 23.04 3332 CB GLN A 544 53.875 −3.348 54.782 1.00 29.05 3333 CG GLN A 544 54.974 −3.219 55.851 1.00 34.54 3334 CD GLN A 544 54.552 −3.697 57.224 1.00 37.02 3335 OE1 GLN A 544 53.442 −3.372 57.648 1.00 39.96 3336 NE2 GLN A 544 55.388 −4.465 57.921 1.00 38.54 3337 N ARG A 545 52.376 −6.121 53.023 1.00 24.22 3338 CA ARG A 545 51.393 −6.420 51.983 1.00 26.56 3339 C ARG A 545 51.405 −5.479 50.781 1.00 22.89 3340 O ARG A 545 50.354 −5.136 50.220 1.00 20.28 3341 CB ARG A 545 49.970 −6.500 52.565 1.00 32.05 3342 CG ARG A 545 49.843 −7.658 53.558 1.00 38.97 3343 CD ARG A 545 48.545 −8.386 53.314 1.00 45.28 3344 NE ARG A 545 47.466 −8.211 54.228 1.00 50.20 3345 CZ ARG A 545 46.728 −7.225 54.696 1.00 52.67 3346 NH1 ARG A 545 46.938 −5.972 54.297 1.00 54.30 3347 NH2 ARG A 545 45.760 −7.508 55.581 1.00 52.76 3348 N ILE A 546 52.568 −4.974 50.391 1.00 19.58 3349 CA ILE A 546 52.691 −4.154 49.197 1.00 18.16 3350 C ILE A 546 53.570 −4.849 48.165 1.00 17.48 3351 O ILE A 546 54.622 −5.411 48.473 1.00 13.86 3352 CB ILE A 546 53.198 −2.730 49.501 1.00 18.44 3353 CG1 ILE A 546 52.267 −2.011 50.485 1.00 18.83 3354 CG2 ILE A 546 53.319 −1.850 48.254 1.00 16.84 3355 CD1 ILE A 546 52.910 −0.740 51.046 1.00 20.08 3356 N GLY A 547 53.077 −4.958 46.936 1.00 16.21 3357 CA GLY A 547 53.802 −5.583 45.845 1.00 13.51 3358 C GLY A 547 54.760 −4.619 45.151 1.00 14.12 3359 O GLY A 547 54.720 −3.383 45.292 1.00 12.19 3360 N VAL A 548 55.614 −5.196 44.275 1.00 11.18 3361 CA VAL A 548 56.557 −4.349 43.534 1.00 11.75 3362 C VAL A 548 56.468 −4.674 42.042 1.00 12.64 3363 O VAL A 548 56.761 −5.829 41.654 1.00 11.98 3364 CB VAL A 548 57.995 −4.621 43.998 1.00 13.59 3365 CG1 VAL A 548 58.998 −3.860 43.135 1.00 15.29 3366 CG2 VAL A 548 58.278 −4.241 45.466 1.00 12.74 3367 N ASN A 549 56.225 −3.678 41.208 1.00 12.65 3368 CA ASN A 549 56.184 −3.878 39.757 1.00 13.79 3369 C ASN A 549 57.405 −3.147 39.191 1.00 15.40 3370 O ASN A 549 57.639 −1.977 39.536 1.00 14.02 3371 CB ASN A 549 54.882 −3.275 39.173 1.00 14.17 3372 CG ASN A 549 53.592 −4.005 39.512 1.00 15.52 3373 OD1 ASN A 549 53.667 −5.127 40.037 1.00 15.71 3374 ND2 ASN A 549 52.374 3.530 39.214 1.00 11.04 3375 N MET A 550 58.240 −3.755 38.342 1.00 14.17 3376 CA MET A 550 59.397 −3.031 37.813 1.00 14.20 3377 C MET A 550 59.099 −2.392 36.448 1.00 14.75 3378 O MET A 550 58.661 −3.107 35.535 1.00 12.87 3379 CB MET A 550 60.626 −3.948 37.655 1.00 13.94 3380 CG MET A 550 61.452 −4.226 38.909 1.00 15.03 3381 SD MET A 550 62.697 −5.561 38.695 1.00 14.47 3382 CE MET A 550 63.764 −4.727 37.472 1.00 16.01 3383 N ASP A 551 59.368 −1.092 36.301 1.00 13.68 3384 CA ASP A 551 59.392 −0.396 35.011 1.00 14.18 3385 C ASP A 551 60.610 −0.949 34.274 1.00 15.34 3386 O ASP A 551 61.711 −0.908 34.871 1.00 16.12 3387 CB ASP A 551 59.565 1.119 35.255 1.00 13.46 3388 CG ASP A 551 59.452 1.990 34.034 1.00 14.83 3389 OD1 ASP A 551 59.595 1.439 32.872 1.00 16.30 3390 OD2 ASP A 551 59.255 3.209 34.103 1.00 12.40 3391 N VAL A 552 60.530 −1.561 33.107 1.00 15.18 3392 CA VAL A 552 61.659 −2.143 32.393 1.00 14.43 3393 C VAL A 552 61.698 −1.675 30.951 1.00 14.19 3394 O VAL A 552 60.693 −1.489 30.256 1.00 15.99 3395 CB VAL A 552 61.674 −3.691 32.386 1.00 14.09 3396 CG1 VAL A 552 62.001 −4.194 33.795 1.00 11.24 3397 CG2 VAL A 552 60.321 −4.237 31.901 1.00 11.60 3398 N VAL A 553 62.900 −1.482 30.427 1.00 13.93 3399 CA VAL A 553 63.153 −0.895 29.128 1.00 15.34 3400 C VAL A 553 63.848 −1.812 28.140 1.00 18.26 3401 O VAL A 553 64.912 −1.514 27.574 1.00 18.77 3402 CB VAL A 553 63.939 0.406 29.373 1.00 14.83 3403 CG1 VAL A 553 64.111 1.249 28.108 1.00 17.28 3404 CG2 VAL A 553 63.326 1.232 30.565 1.00 16.73 3405 N TYR A 554 63.251 −2.945 27.782 1.00 19.23 3406 CA TYR A 554 63.787 −3.864 26.789 1.00 17.41 3407 C TYR A 554 63.647 −3.343 25.367 1.00 17.63 3408 O TYR A 554 64.113 −4.065 24.465 1.00 18.06 3409 CB TYR A 554 63.080 −5.237 26.873 1.00 17.61 3410 CG TYR A 554 63.378 −5.873 28.232 1.00 16.57 3411 CD1 TYR A 554 64.653 −6.384 28.473 1.00 17.67 3412 CD2 TYR A 554 62.423 −5.941 29.222 1.00 16.40 3413 CE1 TYR A 554 64.985 −6.939 29.706 1.00 17.79 3414 CE2 TYR A 554 62.717 −6.544 30.457 1.00 17.52 3415 CZ TYR A 554 64.006 −7.002 30.692 1.00 17.50 3416 OH TYR A 554 64.325 −7.558 31.907 1.00 17.80 3417 N ASN A 555 62.967 −2.210 25.105 1.00 16.07 3418 CA ASN A 555 62.791 −1.817 23.708 1.00 15.21 3419 C ASN A 555 64.017 −1.220 23.038 1.00 15.49 3420 O ASN A 555 63.978 −1.070 21.805 1.00 16.91 3421 CB ASN A 555 61.570 −0.878 23.597 1.00 15.73 3422 CG ASN A 555 61.821 0.417 24.328 1.00 16.71 3423 OD1 ASN A 555 62.555 1.260 23.818 1.00 16.20 3424 ND2 ASN A 555 61.191 0.631 25.511 1.00 15.91 3425 N HIS A 556 65.054 −0.811 23.760 1.00 16.72 3426 CA HIS A 556 66.255 −0.226 23.128 1.00 18.73 3427 C HIS A 556 67.450 −0.203 24.091 1.00 18.92 3428 O HIS A 556 67.155 −0.343 25.279 1.00 20.30 3429 CB HIS A 556 65.917 1.214 22.682 1.00 17.52 3430 CG HIS A 556 65.912 2.220 23.794 1.00 18.40 3431 ND1 HIS A 556 64.764 2.524 24.490 1.00 17.65 3432 CD2 HIS A 556 66.886 2.964 24.365 1.00 18.54 3433 CE1 HIS A 556 65.040 3.431 25.419 1.00 17.28 3434 NE2 HIS A 556 66.303 3.717 25.383 1.00 17.13 3435 N THR A 557 68.719 −0.043 23.692 1.00 18.38 3436 CA THR A 557 69.798 0.042 24.644 1.00 18.28 3437 C THR A 557 70.323 1.476 24.705 1.00 17.57 3438 O THR A 557 69.911 2.301 23.856 1.00 14.70 3339 CB THR A 557 70.926 −0.963 24.352 1.00 19.68 3440 OG1 THR A 557 71.497 −0.474 23.145 1.00 19.18 3441 CG2 THR A 557 70.336 −2.357 24.042 1.00 18.93 3442 N PHE A 558 71.196 1.800 25.663 1.00 16.05 3443 CA PHE A 558 71.758 3.135 25.800 1.00 16.69 3444 C PHE A 558 72.400 3.664 24.505 1.00 18.93 3445 O PHE A 558 72.414 4.873 24.249 1.00 16.69 3446 CB PHE A 558 72.838 3.164 26.910 1.00 16.19 3447 CG PHE A 558 74.193 2.575 26.568 1.00 16.60 3448 CD1 PHE A 558 74.357 1.190 26.467 1.00 16.91 3449 CD2 PHE A 558 75.276 3.376 26.339 1.00 16.22 3450 CE1 PHE A 558 75.602 0.649 26.161 1.00 19.59 3451 CE2 PHE A 558 76.552 2.866 26.027 1.00 16.94 3452 CZ PHE A 558 76.715 1.484 25.941 1.00 18.98 3453 N ASP A 559 72.989 2.777 23.711 1.00 19.99 3454 CA ASP A 559 73.645 3.165 22.465 1.00 24.77 3455 C ASP A 559 73.934 1.880 21.666 1.00 25.09 3456 O ASP A 559 73.574 0.768 22.077 1.00 24.21 3457 CB ASP A 559 74.907 3.979 22.708 1.00 26.93 3458 CG ASP A 559 75.484 4.649 21.466 1.00 31.80 3459 OD1 ASP A 559 76.588 5.194 21.658 1.00 31.12 3460 OD2 ASP A 559 74.883 4.689 20.357 1.00 31.41 3461 N VAL A 560 74.422 2.051 20.464 1.00 24.82 3462 CA VAL A 560 74.699 0.919 19.578 1.00 26.37 3463 C VAL A 560 76.162 0.933 19.226 1.00 26.33 3464 O VAL A 560 76.831 1.966 19.532 1.00 27.51 3465 CB VAL A 560 74.048 1.006 18.185 1.00 29.28 3466 CG1 VAL A 560 72.537 0.936 18.394 1.00 31.23 3467 CG2 VAL A 560 74.398 2.316 17.505 1.00 28.43 3468 N MET A 561 76.781 −0.011 18.554 1.00 26.30 3469 CA MET A 561 78.188 −0.013 18.178 1.00 26.74 3470 C MET A 561 79.185 −0.198 19.320 1.00 26.30 3471 O MET A 561 80.037 −1.085 19.319 1.00 24.56 3472 CB MET A 561 78.547 1.207 17.296 1.00 30.44 3473 CG MET A 561 77.954 0.954 15.881 1.00 34.34 3474 SD MET A 561 78.414 2.299 14.735 1.00 41.54 3475 CE MET A 561 77.950 3.727 15.746 1.00 37.55 3476 N VAL A 562 79.105 0.597 20.392 1.00 24.81 3477 CA VAL A 562 79.878 0.473 21.588 1.00 24.01 3478 C VAL A 562 79.185 −0.465 22.587 1.00 22.04 3479 O VAL A 562 79.767 −0.601 23.647 1.00 22.34 3480 CB VAL A 562 80.058 1.821 22.350 1.00 24.42 3481 CG1 VAL A 562 80.934 2.745 21.496 1.00 24.85 3482 CG2 VAL A 562 78.780 2.479 22.759 1.00 21.36 3483 N SER A 563 78.011 −1.007 22.251 1.00 20.50 3485 CA SER A 563 77.297 −1.820 23.238 1.00 20.03 3485 C SER A 563 77.836 −3.239 23.199 1.00 17.42 3486 O SER A 563 78.348 −3.629 22.143 1.00 17.90 3487 CB SER A 563 75.773 −1.854 23.035 1.00 20.21 3488 OG SER A 563 75.504 −2.439 21.727 1.00 19.79 3489 N ASP A 564 77.647 −3.985 24.276 1.00 15.82 3490 CA ASP A 564 78.065 −5.390 24.327 1.00 15.51 3491 C ASP A 564 77.410 −6.216 23.241 1.00 16.59 3492 O ASP A 564 78.055 −7.027 22.529 1.00 15.21 3493 CB ASP A 564 77.720 −5.977 25.726 1.00 16.55 3494 CG ASP A 564 78.581 −5.296 26.800 1.00 18.34 3495 OD1 ASP A 564 79.821 −5.219 26.651 1.00 17.26 3496 OD2 ASP A 564 78.037 −4.798 27.810 1.00 17.62 3497 N PHE A 565 76.111 −5.973 23.019 1.00 13.96 3498 CA PHE A 565 75.399 −6.655 21.943 1.00 15.67 3499 C PHE A 565 76.139 −6.483 20.599 1.00 14.63 3500 O PHE A 565 76.355 −7.509 19.924 1.00 13.99 3501 CB PHE A 565 73.912 −6.291 21.789 1.00 16.58 3502 CG PHE A 565 72.997 −6.694 22.894 1.00 20.85 3503 CD1 PHE A 565 72.139 −5.782 23.477 1.00 26.06 3504 CD2 PHE A 565 72.967 −7.987 23.380 1.00 23.43 3505 CE1 PHE A 565 71.283 −6.128 24.537 1.00 28.11 3506 CE2 PHE A 565 72.117 −8.352 24.417 1.00 24.43 3507 CZ PHE A 565 71.293 −7.438 25.000 1.00 25.83 3508 N ASP A 566 76.440 −5.285 20.148 1.00 14.36 3509 CA ASP A 566 77.110 −5.056 18.855 1.00 15.72 3510 C ASP A 566 78.563 −5.512 18.779 1.00 17.43 3511 O ASP A 566 79.047 −5.871 17.691 1.00 19.46 3512 CB ASP A 566 77.041 −3.554 18.495 1.00 15.76 3513 CG ASP A 566 75.837 −3.207 17.621 1.00 18.28 3514 OD1 ASP A 566 75.121 −4.134 17.172 1.00 17.60 3515 OD2 ASP A 566 75.529 −1.986 17.464 1.00 18.93 3516 N LYS A 567 79.280 −5.618 19.905 1.00 16.44 3517 CA LYS A 567 80.648 −6.126 19.938 1.00 17.53 3518 C LYS A 567 80.694 −7.648 19.878 1.00 17.64 3519 O LYS A 567 81.712 −8.259 19.540 1.00 17.11 3520 CB LYS A 567 81.414 −5.609 21.194 1.00 17.62 3521 CG LYS A 567 81.622 −4.074 21.089 1.00 18.85 3522 CD LYS A 567 82.538 −3.543 22.204 1.00 18.13 3523 CE LYS A 567 81.848 −3.502 23.564 1.00 18.33 3524 NZ LYS A 567 82.816 −3.195 24.678 1.00 16.66 3525 N ILE A 568 79.612 −8.349 20.201 1.00 16.25 3526 CA ILE A 568 79.549 −9.800 20.123 1.00 16.20 3527 C ILE A 568 78.908 −10.273 18.823 1.00 17.07 3528 O ILE A 568 79.382 −11.238 18.178 1.00 14.48 3529 CB ILE A 568 78.818 −10.362 21.376 1.00 16.15 3530 CG1 ILE A 568 79.514 −9.915 22.665 1.00 15.42 3531 CG2 ILE A 568 78.774 −11.890 21.304 1.00 14.58 3532 CD1 ILE A 568 78.696 −10.199 23.951 1.00 17.78 3533 N VAL A 569 77.730 −9.732 18.434 1.00 15.69 3534 CA VAL A 569 77.048 −10.133 17.196 1.00 15.88 3535 C VAL A 569 76.626 −8.839 16.471 1.00 16.98 3536 O VAL A 569 75.525 −8.306 16.695 1.00 15.04 3537 CB VAL A 569 75.807 −11.021 17.396 1.00 15.85 3538 CG1 VAL A 569 75.416 −11.682 16.074 1.00 14.38 3539 CG2 VAL A 569 75.972 −12.073 18.504 1.00 14.02 3540 N PRO A 570 77.515 −8.315 15.624 1.00 15.25 3541 CA PRO A 570 77.309 −7.021 14.982 1.00 16.13 3542 C PRO A 570 75.950 −6.794 14.359 1.00 16.17 3543 O PRO A 570 75.466 −7.600 13.555 1.00 15.22 3544 CB PRO A 570 78.472 −6.901 14.010 1.00 17.25 3545 CG PRO A 570 79.570 −7.724 14.640 1.00 16.61 3546 CD PRO A 570 78.844 −8.878 15.311 1.00 15.81 3547 N GLN A 571 75.257 −5.746 14.775 1.00 14.50 3548 CA GLN A 571 73.918 −5.303 14.447 1.00 14.80 3549 C GLN A 571 72.705 −6.160 14.739 1.00 16.27 3550 O GLN A 571 71.549 −5.639 14.722 1.00 13.56 3551 CB GLN A 571 73.748 −4.892 12.953 1.00 15.26 3552 CG GLN A 571 74.766 −3.823 12.497 1.00 15.43 3553 CD GLN A 571 74.503 −3.354 11.059 1.00 19.19 3554 OE1 GLN A 571 73.563 −3.777 10.388 1.00 18.40 3555 NE2 GLN A 571 75.367 −2.510 10.508 1.00 16.57 3556 N TYR A 572 72.855 −7.469 14.886 1.00 16.66 3557 CA TYR A 572 71.762 −8.426 14.967 1.00 16.46 3558 C TYR A 572 70.762 −8.214 16.097 1.00 15.79 3559 O TYR A 572 69.571 −8.534 15.888 1.00 15.97 3560 CB TYR A 572 72.356 −9.851 15.074 1.00 15.56 3561 CG TYR A 572 71.265 −10.918 14.864 1.00 16.45 3562 CD1 TYR A 572 70.668 −11.104 13.618 1.00 15.36 3563 CD2 TYR A 572 70.776 −11.624 15.938 1.00 15.32 3564 CE1 TYR A 572 69.678 −12.067 13.462 1.00 16.37 3565 CE2 TYR A 572 69.793 −12.590 15.799 1.00 16.69 3566 CZ TYR A 572 69.237 −12.809 14.543 1.00 16.67 3567 OH TYR A 572 68.200 −13.718 14.410 1.00 15.39 3568 N TYR A 573 71.134 −7.671 17.246 1.00 16.43 3569 CA TYR A 573 70.136 −7.459 18.322 1.00 17.97 3570 C TYR A 573 69.259 −6.225 18.096 1.00 17.17 3571 O TYR A 573 68.347 −5.946 18.884 1.00 13.58 3572 CB TYR A 573 70.852 −7.342 19.679 1.00 18.07 3573 CG TYR A 573 71.414 −8.647 20.227 1.00 20.16 3574 CD1 TYR A 573 72.722 −9.044 20.012 1.00 19.58 3575 CD2 TYR A 573 70.603 −9.487 21.008 1.00 20.25 3576 CE1 TYR A 573 73.204 −10.247 20.549 1.00 20.41 3577 CE2 TYR A 573 71.064 −10.682 21.552 1.00 19.87 3578 CZ TYR A 573 72.388 −11.041 21.317 1.00 20.91 3579 OH TYR A 573 72.862 −12.222 21.864 1.00 20.44 3580 N TYR A 574 69.515 −5.474 17.014 1.00 16.82 3581 CA TYR A 574 68.727 −4.275 16.718 1.00 15.66 3582 C TYR A 574 68.004 −4.350 15.382 1.00 16.73 3583 O TYR A 574 68.406 −5.134 14.504 1.00 18.00 3584 CB TYR A 574 69.665 −3.067 16.759 1.00 15.38 3585 CG TYR A 574 70.493 −2.931 18.020 1.00 18.02 3586 CD1 TYR A 574 69.924 −2.327 19.156 1.00 17.70 3587 CD2 TYR A 574 71.787 −3.466 18.124 1.00 18.97 3588 CE1 TYR A 574 70.640 −2.205 20.327 1.00 16.27 3589 CE2 TYR A 574 72.507 −3.336 19.319 1.00 18.59 3590 CZ TYR A 574 71.932 −2.685 20.399 1.00 18.97 3591 OH TYR A 574 72.633 −2.523 21.588 1.00 18.86 3592 N ARG A 575 66.949 −3.552 15.167 1.00 14.99 3593 CA ARG A 575 66.271 −3.493 13.869 1.00 15.92 3594 C ARG A 575 66.986 −2.557 12.896 1.00 16.49 3595 O ARG A 575 67.443 −1.428 13.268 1.00 14.85 3596 CB ARG A 575 64.798 −3.050 14.073 1.00 15.06 3597 CG ARG A 575 63.996 −3.916 15.070 1.00 15.88 3598 CD ARG A 575 62.468 −3.788 14.882 1.00 16.88 3599 NE ARG A 575 61.750 −4.691 15.785 1.00 13.65 3600 CZ ARG A 575 61.087 −4.506 16.914 1.00 16.15 3601 NH1 ARG A 575 60.840 −3.302 17.495 1.00 13.01 3602 NH2 ARG A 575 60.591 −5.606 17.516 1.00 11.72 3603 N THR A 576 67.240 −3.018 11.669 1.00 17.48 3604 CA THR A 576 67.911 −2.206 10.648 1.00 16.92 3605 C THR A 576 67.062 −2.149 9.365 1.00 18.54 3606 O THR A 576 66.283 −3.087 9.134 1.00 19.15 3607 CB THR A 576 69.304 −2.708 10.228 1.00 17.51 3608 OG1 THR A 576 69.224 −4.053 9.768 1.00 12.75 3609 CG2 THR A 576 70.351 −2.561 11.345 1.00 18.13 3610 N ASP A 577 67.206 −1.088 8.567 1.00 18.10 3611 CA ASP A 577 66.406 −0.999 7.351 1.00 18.80 3612 C ASP A 577 67.218 −1.512 6.154 1.00 20.47 3613 O ASP A 577 68.348 −2.037 6.306 1.00 22.66 3614 CB ASP A 577 65.858 0.404 7.051 1.00 18.16 3615 CG ASP A 577 66.941 1.424 6.856 1.00 19.10 3616 OD1 ASP A 577 66.636 2.634 7.169 1.00 19.08 3617 CD2 ASP A 577 68.119 1.198 6.485 1.00 16.70 3618 N SER A 578 66.674 −1.364 4.963 1.00 20.77 3619 CA SER A 578 67.276 −1.837 3.705 1.00 21.43 3620 C SER A 578 68.503 −1.061 3.308 1.00 21.24 3621 O SER A 578 69.334 −1.575 2.544 1.00 21.58 3622 CB SER A 578 66.212 −1.815 2.599 1.00 23.81 3623 OG SER A 578 65.419 −2.993 2.665 1.00 24.09 3624 N ASN A 579 68.692 0.150 3.800 1.00 21.04 3625 CA ASN A 579 69.893 0.918 3.551 1.00 22.84 3626 C ASN A 579 71.069 0.581 4.470 1.00 22.28 3627 O ASN A 579 72.244 1.070 4.370 1.00 22.77 3628 CB ASN A 579 69.572 2.403 3.670 1.00 24.77 3629 CG ASN A 579 68.611 2.929 2.641 1.00 27.96 3630 OD1 ASN A 579 67.940 3.947 2.900 1.00 30.34 3631 ND2 ASN A 579 68.431 2.198 1.548 1.00 27.67 3632 N GLY A 580 70.811 −0.191 5.501 1.00 21.69 3633 CA GLY A 580 71.749 −0.563 6.551 1.00 20.67 3634 C GLY A 580 71.708 0.335 7.781 1.00 20.28 3635 O GLY A 580 72.723 0.373 8.505 1.00 20.34 3636 N ASN A 581 70.727 1.230 7.907 1.00 19.77 3637 CA ASN A 581 70.647 2.096 9.057 1.00 20.14 3638 C ASN A 581 69.811 1.448 10.186 1.00 20.05 3639 O ASN A 581 68.809 0.802 9.843 1.00 20.06 3640 CB ASN A 581 70.061 3.486 8.758 1.00 20.77 3641 CG ASN A 581 70.979 4.271 7.815 1.00 24.55 3642 OD1 ASN A 581 72.201 4.336 7.991 1.00 25.71 3643 ND2 ASN A 581 70.436 4.847 6.760 1.00 22.88 3644 N TYR A 582 70.211 1.744 11.428 1.00 18.90 3645 CA TYR A 582 69.377 1.345 12.592 1.00 20.45 3646 C TYR A 582 68.045 2.071 12.591 1.00 18.67 3647 O TYR A 582 68.050 3.319 12.396 1.00 17.45 3648 CB TYR A 582 70.093 1.730 13.900 1.00 21.60 3649 CG TYR A 582 71.394 0.997 14.143 1.00 26.25 3650 CD1 TYR A 582 72.639 1.501 13.726 1.00 27.97 3651 CD2 TYR A 582 71.374 −0.230 14.777 1.00 27.31 3652 CE1 TYR A 582 73.853 0.831 13.960 1.00 28.48 3653 CE2 TYR A 582 72.561 −0.924 15.000 1.00 28.99 3654 CZ TYR A 582 73.774 −0.390 14.589 1.00 28.99 3655 OH TYR A 582 74.899 −1.115 14.864 1.00 28.24 3656 N THR A 583 66.912 1.437 12.737 1.00 18.57 3657 CA THR A 583 65.623 2.143 12.764 1.00 19.17 3658 C THR A 583 65.399 2.672 14.204 1.00 19.21 3659 O THR A 583 66.002 2.240 15.227 1.00 15.73 3660 CB THR A 583 64.442 1.271 12.295 1.00 21.01 3661 OG1 THR A 583 64.334 0.091 13.179 1.00 19.15 3662 CG2 THR A 583 64.598 0.758 10.847 1.00 20.19 3663 N ASN A 584 64.574 3.728 14.303 1.00 16.30 3664 CA ASN A 584 64.420 4.507 15.514 1.00 17.48 3665 C ASN A 584 63.063 4.434 16.164 1.00 17.05 3666 O ASN A 584 62.469 5.447 16.559 1.00 16.19 3667 CB ASN A 584 64.779 5.966 15.133 1.00 19.28 3668 CG ASN A 584 65.141 6.823 16.319 1.00 20.58 3669 OD1 ASN A 584 65.304 6.339 17.435 1.00 22.86 3670 ND2 ASN A 584 65.101 8.148 16.199 1.00 22.27 3671 N GLY A 585 62.499 3.249 16.338 1.00 17.36 3672 CA GLY A 585 61.169 3.095 16.940 1.00 18.20 3673 C GLY A 585 61.073 3.688 18.348 1.00 19.43 3674 O GLY A 585 60.000 4.151 18.739 1.00 17.42 3675 N SER A 586 62.149 3.685 19.128 1.00 20.93 3676 CA SER A 586 62.095 4.195 20.490 1.00 21.54 3677 C SER A 586 62.259 5.711 20.590 1.00 20.81 3678 O SER A 586 61.993 6.277 21.652 1.00 20.13 3679 CB SER A 586 63.221 3.538 21.302 1.00 20.63 3680 OG SER A 586 64.491 4.039 20.840 1.00 21.23 3681 N GLY A 587 62.771 6.354 19.558 1.00 19.63 3682 CA GLY A 587 63.102 7.781 19.629 1.00 20.56 3683 C GLY A 587 64.469 8.006 20.279 1.00 21.87 3684 O GLY A 587 64.930 9.158 20.346 1.00 21.43 3685 N CYS A 588 65.213 6.945 20.630 1.00 19.06 3686 CA CYS A 588 66.495 7.043 21.300 1.00 19.09 3687 C CYS A 588 67.651 6.569 20.417 1.00 20.16 3688 O CYS A 588 68.797 6.442 20.864 1.00 18.88 3689 CB CYS A 588 66.462 6.167 22.569 1.00 18.06 3690 SG CYS A 588 65.249 6.772 23.792 1.00 20.94 3691 N GLY A 589 67.358 6.343 19.130 1.00 19.74 3692 CA GLY A 589 68.464 5.999 18.224 1.00 20.77 3693 C GLY A 589 68.511 4.521 17.843 1.00 20.75 3694 O GLY A 589 69.319 4.222 16.957 1.00 21.38 3695 N ASN A 590 67.768 3.611 18.454 1.00 18.78 3696 CA ASN A 590 67.823 2.183 18.077 1.00 17.60 3697 C ASN A 590 66.576 1.529 18.652 1.00 17.96 3698 O ASN A 590 65.865 2.190 19.463 1.00 17.56 3699 CB ASN A 590 69.087 1.484 18.624 1.00 15.88 3700 CG ASN A 590 69.144 1.355 20.139 1.00 17.35 3701 OD1 ASN A 590 68.469 0.536 20.774 1.00 15.30 3702 ND2 ASN A 590 69.897 2.207 20.808 1.00 15.71 3703 N GLU A 591 66.335 0.275 18.302 1.00 17.77 3704 CA GLU A 591 65.200 −0.435 18.873 1.00 18.01 3705 C GLU A 591 65.575 −1.923 18.828 1.00 18.01 3706 O GLU A 591 66.264 −2.419 17.909 1.00 17.69 3707 CB GLU A 591 63.831 −0.072 18.251 1.00 19.26 3708 CG GLU A 591 63.658 −0.382 16.805 1.00 18.33 3709 CD GLU A 591 62.322 −0.090 16.134 1.00 19.76 3710 OE1 GLU A 591 62.383 0.617 15.092 1.00 18.91 3711 OE2 GLU A 591 61.249 −0.589 16.551 1.00 18.36 3712 N PHE A 592 65.262 −2.635 19.900 1.00 15.35 3713 CA PHE A 592 65.646 −4.041 20.070 1.00 18.51 3714 C PHE A 592 64.787 −4.958 19.219 1.00 16.58 3715 O PHE A 592 63.532 −4.916 19.203 1.00 18.31 3716 CB PHE A 592 65.507 −4.390 21.572 1.00 18.66 3717 CG PHE A 592 66.320 −5.575 22.007 1.00 19.55 3718 CD1 PHE A 592 67.687 −5.484 22.227 1.00 21.67 3719 CD2 PHE A 592 65.700 −6.800 22.204 1.00 21.14 3720 CE1 PHE A 592 66.400 −6.593 22.666 1.00 21.13 3721 CE2 PHE A 592 66.399 −7.894 22.657 1.00 21.68 3722 CZ PHE A 592 67.750 −7.786 22.877 1.00 20.22 3723 N ALA A 593 65.422 −5.805 18.433 1.00 15.23 3724 CA ALA A 593 64.731 −6.643 17.459 1.00 14.58 3725 C ALA A 593 64.218 −7.941 18.052 1.00 15.78 3726 O ALA A 593 64.818 −8.986 17.839 1.00 15.37 3727 CB ALA A 593 65.653 −6.921 16.263 1.00 14.49 3728 N THR A 594 63.084 −7.909 18.737 1.00 13.64 3729 CA THR A 594 62.430 −9.049 19.319 1.00 17.21 3730 C THR A 594 61.898 −10.007 18.255 1.00 18.41 3731 O THR A 594 61.673 −11.162 18.635 1.00 16.76 3732 CB THR A 594 61.234 −8.677 20.250 1.00 15.31 3733 OG1 THR A 594 60.306 −7.885 19.481 1.00 16.09 3734 CG2 THR A 594 61.715 −7.890 21.453 1.00 15.49 3735 N GLU A 595 61.862 −9.680 16.956 1.00 17.58 3736 CA GLU A 595 61.519 −10.670 15.952 1.00 17.42 3737 C GLU A 595 62.715 −11.589 15.648 1.00 18.14 3738 O GLU A 595 62.627 −12.532 14.859 1.00 19.18 3739 CB GLU A 595 60.966 −10.097 14.646 1.00 18.92 3740 CG GLU A 595 61.955 −9.284 13.797 1.00 17.41 3741 CD GLU A 595 62.217 −7.889 14.333 1.00 18.02 3742 OE1 GLU A 595 61.964 −7.461 15.493 1.00 16.28 3743 OE2 GLU A 595 62.768 −7.075 13.557 1.00 18.81 3744 N HIS A 596 63.900 −11.351 16.189 1.00 16.45 3745 CA HIS A 596 65.050 −12.239 15.996 1.00 15.59 3746 C HIS A 596 65.076 −13.182 17.190 1.00 16.08 3747 O HIS A 596 65.031 −12.701 18.324 1.00 15.72 3748 CB HIS A 596 66.324 −11.404 15.934 1.00 14.25 3749 CG HIS A 596 66.598 −10.769 14.592 1.00 16.18 3750 ND1 HIS A 596 67.579 −9.788 14.434 1.00 14.53 3751 CD2 HIS A 596 66.014 −10.918 13.388 1.00 13.81 3752 CE1 HIS A 596 67.617 −9.420 13.163 1.00 15.09 3753 NE2 HIS A 596 66.708 −10.116 12.524 1.00 15.29 3754 N PRO A 597 64.965 −14.485 16.976 1.00 16.49 3755 CA PRO A 597 64.763 −15.436 18.023 1.00 17.55 3756 C PRO A 597 65.654 −15.307 19.250 1.00 18.38 3757 O PRO A 597 65.097 −15.446 20.358 1.00 17.58 3758 CB PRO A 597 64.928 −16.799 17.319 1.00 17.50 3759 CG PRO A 597 64.306 −16.514 15.953 1.00 18.51 3760 CD PRO A 597 64.817 −15.129 15.637 1.00 18.53 3761 N MET A 598 66.964 −15.173 19.087 1.00 15.98 3762 CA MET A 598 67.874 −15.133 20.231 1.00 15.82 3763 C MET A 598 67.729 −13.791 20.940 1.00 15.34 3764 O MET A 598 68.082 −13.708 22.130 1.00 16.95 3765 CB MET A 598 69.336 −15.412 19.803 1.00 16.00 3766 CG MET A 598 69.574 −16.841 19.325 1.00 13.68 3767 SD MET A 598 69.207 −18.085 20.579 1.00 13.98 3768 CE MET A 598 70.593 −17.828 21.697 1.00 15.11 3769 N ALA A 599 67.344 −12.740 20.202 1.00 14.72 3770 CA ALA A 599 67.059 −11.481 20.876 1.00 15.20 3771 C ALA A 599 65.783 −11.665 21.708 1.00 16.47 3772 O ALA A 599 65.749 −11.281 22.874 1.00 17.10 3773 CB ALA A 599 66.943 −10.328 19.898 1.00 13.55 3774 N GLN A 600 64.731 −12.308 21.178 1.00 16.72 3775 CA GLN A 600 63.525 −12.575 21.946 1.00 18.51 3776 C GLN A 600 63.860 −13.406 23.201 1.00 17.76 3777 O GLN A 600 63.429 −13.048 24.311 1.00 13.69 3778 CB GLN A 600 62.404 −13.240 21.137 1.00 17.71 3779 CG GLN A 600 61.117 −13.534 21.935 1.00 16.56 3780 CD GLN A 600 60.174 −14.357 21.052 1.00 16.99 3781 OE1 GLN A 600 60.365 −15.573 20.886 1.00 17.99 3782 NE2 GLN A 600 59.383 −13.690 20.475 1.00 12.76 3783 N LYS A 601 64.723 −14.418 23.042 1.00 17.63 3784 CA LYS A 601 65.138 −15.279 24.130 3.00 17.70 3785 C LYS A 601 65.881 −14.491 25.221 1.00 18.25 3786 O LYS A 601 65.662 −14.783 26.399 1.00 16.32 3787 CB LYS A 601 66.023 −16.457 23.633 1.00 38.32 3788 CG LYS A 601 66.619 −17.286 24.778 1.00 17.88 3789 CD LYS A 601 67.393 −18.512 24.279 1.00 18.60 3790 CE LYS A 601 68.237 −19.167 25.397 1.00 18.85 3791 NZ LYS A 601 67.398 −19.618 26.571 1.00 16.70 3792 N PHE A 602 66.732 −13.517 24.854 1.00 17.63 3793 CA PHE A 602 67.370 −12.649 25.854 1.00 16.13 3794 C PHE A 602 66.329 −12.012 26.764 1.00 16.27 3795 O PHE A 602 66.554 −11.907 28.009 1.00 14.81 3796 CB PHE A 602 68.204 −11.538 25.161 1.00 16.06 3797 CG PHE A 602 68.846 −10.590 26.149 1.00 16.65 3798 CD1 PHE A 602 68.244 −9.406 26.531 3.00 15.22 3799 CD2 PHE A 602 70.050 −10.983 26.751 1.00 17.45 3800 CE1 PHE A 602 68.808 −8.625 27.539 1.00 16.75 3801 CE2 PHE A 602 70.620 −10.203 27.747 1.00 17.98 3802 CZ PHE A 602 70.006 −9.011 28.135 1.00 15.11 3803 N VAL A 603 65.258 −11.426 26.371 1.00 15.45 3804 CA VAL A 603 64.237 −10.777 27.017 1.00 15.99 3805 C VAL A 603 63.494 −11.778 27.884 1.00 16.06 3806 O VAL A 603 63.332 −11.545 29.095 1.00 16.02 3807 CB VAL A 603 63.212 −9.946 26.186 1.00 18.42 3808 CG1 VAL A 603 62.219 −9.197 27.073 1.00 14.68 3809 CG2 VAL A 603 63.961 −8.957 25.276 1.00 15.72 3810 N LEU A 604 63.039 −12.897 27.353 1.00 13.96 3811 CA LEU A 604 62.322 −13.923 28.086 1.00 15.23 3812 C LEU A 604 63.112 −14.470 29.269 1.00 37.26 3813 O LEU A 604 62.593 −14.609 30.374 1.00 14.68 3814 CB LEU A 604 61.903 −15.076 27.150 1.00 18.02 3815 CG LEU A 604 60.794 −14.774 26.119 1.00 19.15 3816 CD1 LEU A 604 60.645 −15.892 25.085 1.00 19.70 3817 CD2 LEU A 604 59.464 −14.593 26.844 1.00 23.10 3818 N ASP A 605 64.415 −14.727 29.072 1.00 15.26 3819 CA ASP A 605 65.335 −15.216 30.095 1.00 16.47 3820 C ASP A 605 65.424 −14.164 31.216 1.00 16.78 3821 O ASP A 605 65.426 −14.517 32.390 1.00 15.91 3822 CB ASP A 605 66.722 −15.477 29.523 1.00 14.57 3823 CG ASP A 605 66.881 −16.749 28.698 1.00 18.15 3824 OD1 ASP A 605 67.938 −16.953 28.012 1.00 14.80 3825 OD2 ASP A 605 65.927 −17.564 28.720 1.00 15.40 3826 N SER A 606 65.555 −12.903 30.809 1.00 15.59 3827 CA SER A 606 65.736 −11.772 31.721 1.00 14.83 3828 C SER A 606 64.501 −31.560 32.614 1.00 14.39 3829 O SER A 606 64.675 −11.460 33.840 1.00 13.45 3830 CB SER A 606 66.094 −10.483 30.977 1.00 14.58 3831 OG SER A 606 66.281 −9.390 31.898 1.00 14.28 3832 N VAL A 607 63.265 −11.480 32.095 1.00 14.64 3833 CA VAL A 607 62.127 −11.281 33.004 1.00 15.38 3834 C VAL A 607 61.945 −12.521 33.896 1.00 15.96 3835 O VAL A 607 61.514 −12.318 35.035 1.00 15.28 3836 CB VAL A 607 60.810 −10.937 32.280 1.00 15.47 3837 CG1 VAL A 607 60.974 −9.551 31.618 1.00 13.07 3838 CG2 VAL A 607 60.425 −12.035 31.284 1.00 12.85 3839 N ASN A 608 62.193 −13.746 33.446 1.00 14.92 3840 CA ASN A 608 62.161 −14.916 34.299 1.00 16.74 3841 C ASN A 608 63.201 −14.835 35.444 1.00 17.85 3842 O ASN A 608 62.877 −15.128 36.608 1.00 17.58 3843 CB ASN A 608 62.493 −16.209 33.518 1.00 19.59 3844 CG ASN A 608 61.296 −16.876 32.872 1.00 22.08 3845 OD1 ASN A 608 60.979 −16.711 31.678 1.00 25.08 3846 ND2 ASN A 608 60.495 −17.611 33.626 1.00 20.95 3847 N TYR A 609 64.415 −14.328 35.175 1.00 15.99 3848 CA TYR A 609 65.427 −14.137 36.228 1.00 15.94 3849 C TYR A 609 64.972 −13.130 37.284 1.00 17.05 3850 O TYR A 609 65.128 −13.371 38.504 1.00 15.91 3851 CB TYR A 609 66.775 −13.708 35.575 1.00 15.56 3852 CG TYR A 609 67.853 −13.313 36.573 1.00 16.22 3853 CD1 TYR A 609 68.489 −14.266 37.390 1.00 16.45 3854 CD2 TYR A 609 68.197 −12.002 36.736 1.00 16.36 3855 CE1 TYR A 609 69.470 −13.877 38.289 1.00 17.53 3856 CE2 TYR A 609 69.169 −11.603 37.661 1.00 17.03 3857 CZ TYR A 609 69.731 −12.544 38.487 1.00 17.07 3858 OH TYR A 609 70.710 −12.140 39.389 1.00 18.77 3859 N TRP A 610 64.391 −11.975 36.873 1.00 15.33 3860 CA TRP A 610 63.997 −10.954 37.843 1.00 14.87 3861 C TRP A 610 62.906 −11.516 38.749 1.00 17.00 3862 O TRP A 610 62.946 −11.295 39.934 1.00 15.43 3863 CB TRP A 610 63.571 −9.617 37.205 1.00 16.60 3864 CG TRP A 610 64.795 −8.841 36.758 1.00 17.32 3865 CD1 TRP A 610 65.385 −8.826 35.530 1.00 18.14 3866 CD2 TRP A 610 65.604 −8.000 37.606 1.00 16.87 3867 NE1 TRP A 610 66.501 −8.032 35.528 1.00 17.52 3868 CE2 TRP A 610 66.670 −7.524 36.816 1.00 17.86 3869 CE3 TRP A 610 65.507 −7.619 38.949 1.00 16.40 3870 CZ2 TRP A 610 67.624 −6.629 37.310 1.00 17.05 3871 CZ3 TRP A 610 66.480 −6.768 39.473 1.00 18.04 3872 CH2 TRP A 610 67.519 −6.256 38.646 1.00 16.76 3873 N VAL A 611 61.917 −12.259 38.217 1.00 17.68 3874 CA VAL A 611 60.891 −12.872 39.051 1.00 17.19 3875 C VAL A 611 61.481 −13.944 39.976 1.00 17.50 3876 O VAL A 611 61.150 −13.951 41.159 1.00 17.52 3877 CB VAL A 611 59.784 −13.473 38.166 1.00 16.45 3878 CG1 VAL A 611 58.825 −14.397 38.941 1.00 13.42 3879 CG2 VAL A 611 58.959 −12.335 37.537 1.00 15.16 3880 N ASN A 612 62.221 −14.917 39.491 1.00 17.95 3881 CA ASN A 612 62.770 −15.986 40.314 1.00 19.97 3882 C ASN A 612 63.769 −15.479 41.361 1.00 20.64 3883 O ASN A 612 63.629 −15.773 42.566 1.00 19.49 3884 CB ASN A 612 63.350 −17.062 39.398 1.00 23.07 3885 CG ASN A 612 62.330 −17.925 38.661 1.00 27.67 3886 OD1 ASN A 612 62.706 −18.413 37.561 1.00 30.76 3887 ND2 ASN A 612 61.091 −18.211 39.114 1.00 23.39 3888 N GLU A 613 64.794 −14.722 40.987 1.00 17.75 3889 CA GLU A 613 65.784 −14.237 41.933 1.00 16.91 3890 C GLU A 613 65.325 −13.120 42.851 1.00 16.20 3891 O GLU A 613 65.810 −13.011 44.017 1.00 15.78 3892 CB GLU A 613 67.044 −13.805 41.121 1.00 17.72 3893 CG GLU A 613 68.292 −13.483 41.942 1.00 17.78 3894 CD GLU A 613 68.895 −14.683 42.660 1.00 19.51 3895 OE1 GLU A 613 68.818 −15.820 42.180 1.00 18.15 3896 OE2 GLU A 613 69.413 −14.521 43.782 1.00 21.38 3897 N TYR A 614 64.583 −12.123 42.358 1.00 14.53 3898 CA TYR A 614 64.252 −10.958 43.180 1.00 14.18 3899 C TYR A 614 62.805 −11.002 43.696 1.00 17.41 3900 O TYR A 614 62.446 −10.102 44.461 1.00 17.30 3901 CB TYR A 614 64.553 −9.677 42.390 1.00 13.30 3902 CG TYR A 614 66.058 −9.370 42.201 1.00 14.37 3903 CD1 TYR A 614 66.759 −8.589 43.088 1.00 14.58 3904 CD2 TYR A 614 66.753 −9.907 41.128 1.00 13.92 3905 CE1 TYR A 614 68.139 −8.317 42.936 1.00 14.22 3906 CE2 TYR A 614 68.120 −9.659 40.942 1.00 13.85 3907 CZ TYR A 614 68.795 −8.864 41.857 1.00 15.00 3908 OH TYR A 614 70.152 −8.611 41.699 1.00 13.86 3909 N HIS A 615 61.982 −11.968 43.309 1.00 16.00 3910 CA HIS A 615 60.589 −12.094 43.716 1.00 18.34 3911 C HIS A 615 59.671 −10.919 43.363 1.00 18.85 3912 O HIS A 615 58.762 −10.588 44.142 1.00 19.15 3913 CB HIS A 615 60.472 −12.330 45.226 1.00 19.79 3914 CG HIS A 615 61.244 −13.480 45.789 1.00 21.80 3915 ND1 HIS A 615 61.349 −13.681 47.151 1.00 22.61 3916 CD2 HIS A 615 62.034 −14.415 45.189 1.00 23.99 3917 CE1 HIS A 615 62.102 −14.765 47.345 1.00 24.07 3918 NE2 HIS A 615 62.561 −15.201 46.179 1.00 24.55 3919 N VAL A 616 59.898 −10.221 42.256 1.00 19.10 3920 CA VAL A 616 59.090 −9.071 41.856 1.00 18.87 3921 C VAL A 616 57.723 −9.605 41.412 1.00 18.87 3922 O VAL A 616 57.590 −10.767 41.010 1.00 16.35 3923 CB VAL A 616 59.829 −8.264 40.774 1.00 21.79 3924 CG1 VAL A 616 61.242 −7.865 41.282 1.00 19.85 3925 CG2 VAL A 616 59.980 −9.080 39.511 1.00 22.01 3926 N ASP A 617 56.694 −8.777 41.512 1.00 16.55 3927 CA ASP A 617 55.309 −9.174 41.337 1.00 17.29 3928 C ASP A 617 54.694 −8.774 39.989 1.00 17.05 3929 O ASP A 617 53.493 −9.039 39.778 1.00 14.04 3930 CB ASP A 617 54.484 −8.457 42.450 1.00 15.59 3931 CG ASP A 617 55.057 −8.762 43.825 1.00 18.73 3932 OD1 ASP A 617 55.655 −7.918 44.531 1.00 18.45 3933 OD2 ASP A 617 54.889 −9.919 44.243 1.00 17.15 3934 N GLY A 618 55.464 −8.049 39.176 1.00 15.87 3935 CA GLY A 618 54.873 −7.628 37.888 1.00 16.30 3936 C GLY A 618 55.813 −6.711 37.149 1.00 15.89 3937 O GLY A 618 56.907 −6.366 37.645 1.00 16.86 3938 N PHE A 619 55.484 −6.362 35.912 1.00 15.02 3939 CA PHE A 619 56.312 −5.472 35.083 1.00 14.50 3940 C PHE A 619 55.488 −4.376 34.420 1.00 15.17 3941 O PHE A 619 54.403 −4.681 33.856 1.00 13.52 3942 CB PHE A 619 56.997 −6.325 33.956 1.00 14.48 3943 CG PHE A 619 58.073 −7.230 34.506 1.00 16.81 3944 CD1 PHE A 619 59.281 −6.690 34.973 1.00 16.56 3945 CD2 PHE A 619 57.858 −8.593 34.669 1.00 16.67 3946 CE1 PHE A 619 60.255 −7.484 35.545 1.00 15.02 3947 CE2 PHE A 619 58.854 −9.403 35.213 1.00 15.82 3948 CZ PHE A 619 60.044 −8.841 35.642 1.00 15.77 3949 N ARG A 620 56.013 −3.165 34.311 1.00 13.06 3950 CA ARG A 620 55.491 −2.106 33.449 1.00 14.20 3951 C ARG A 620 56.455 −1.959 32.251 1.00 13.44 3952 O ARG A 620 57.627 −1.593 32.444 1.00 12.26 3953 CB ARG A 620 55.343 −0.758 34.177 1.00 14.29 3954 CG ARG A 620 55.098 0.479 33.294 1.00 14.46 3955 CD ARG A 620 56.325 1.383 33.136 1.00 15.20 3956 NE ARG A 620 55.937 2.660 32.513 1.00 16.32 3957 CZ ARG A 620 56.625 3.360 31.605 1.00 17.13 3958 NH1 ARG A 620 57.796 2.947 31.125 1.00 13.61 3959 NH2 ARG A 620 56.155 4.529 31.132 1.00 15.70 3960 N PHE A 621 56.083 −2.274 31.031 1.00 14.29 3961 CA PHE A 621 56.956 −2.250 29.884 1.00 16.71 3962 C PHE A 621 56.956 −0.918 29.145 1.00 17.64 3963 O PHE A 621 55.903 −0.563 28.593 1.00 16.47 3964 CB PHE A 621 56.636 −3.381 28.868 1.00 17.26 3965 CG PHE A 621 56.868 −4.750 29.455 1.00 17.89 3966 CD1 PHE A 621 58.079 −5.403 29.341 1.00 15.81 3967 CD2 PHE A 621 55.812 −5.373 30.137 1.00 17.10 3968 CE1 PHE A 621 58.263 −6.641 29.911 1.00 16.43 3969 CE2 PHE A 621 56.005 −6.626 30.688 1.00 16.26 3970 CZ PHE A 621 57.224 −7.266 30.597 1.00 15.91 3971 N ASP A 622 58.055 −0.182 29.255 1.00 16.73 3972 CA ASP A 622 58.232 1.100 28.539 1.00 17.39 3973 C ASP A 622 57.977 0.876 27.031 1.00 17.25 3974 O ASP A 622 58.434 −0.189 26.565 1.00 14.93 3975 CB ASP A 622 59.739 1.393 28.604 1.00 16.80 3976 CG ASP A 622 60.044 2.811 28.095 1.00 18.67 3977 OD1 ASP A 622 59.447 3.734 28.683 1.00 16.60 3978 OD2 ASP A 622 60.871 2.977 27.145 1.00 18.13 3979 N LEU A 623 57.278 1.764 26.338 1.00 14.28 3980 CA LEU A 623 56.984 1.619 24.923 1.00 15.86 3981 C LEU A 623 56.733 0.197 24.536 1.00 15.06 3982 O LEU A 623 57.346 −0.346 23.597 1.00 16.48 3983 CB LEU A 623 58.151 2.214 24.052 1.00 14.51 3984 CG LEU A 623 58.401 3.692 24.416 1.00 16.34 3985 CD1 LEU A 623 59.675 4.160 23.681 1.00 16.33 3986 CD2 LEU A 623 57.188 4.593 24.089 1.00 13.45 3987 N MET A 624 55.835 −0.489 25.247 1.00 15.49 3988 CA MET A 624 55.522 −1.877 25.003 1.00 13.19 3989 C MET A 624 55.102 −2.198 23.584 1.00 16.10 3990 O MET A 624 55.275 −3.346 23.112 1.00 13.77 3991 CB MET A 624 54.406 −2.290 25.999 1.00 14.22 3992 CG MET A 624 54.070 −3.777 26.030 1.00 14.94 3993 SD MET A 624 52.577 −4.324 27.305 1.00 14.57 3994 CE MET A 624 51.421 −3.499 26.628 1.00 14.71 3995 N ALA A 625 54.506 −1.234 22.820 1.00 15.88 3996 CA ALA A 525 54.068 −1.599 21.477 1.00 16.48 3997 C ALA A 625 55.250 −2.159 20.679 1.00 16.42 3998 O ALA A 625 55.086 −3.090 19.890 1.00 14.03 3999 CB ALA A 625 53.509 −0.409 20.706 1.00 16.88 4000 N LEU A 626 56.430 −1.595 20.853 1.00 16.65 4001 CA LEU A 626 57.627 −2.049 20.152 1.00 17.27 4002 C LEU A 626 58.090 −3.482 20.395 1.00 18.21 4003 O LEU A 626 58.839 −4.029 19.551 1.00 18.64 4004 CB LEU A 626 58.766 −1.121 20.566 1.00 17.52 4005 CG LEU A 626 58.661 0.383 20.154 1.00 17.88 4006 CD1 LEU A 626 59.903 1.092 20.758 1.00 16.85 4007 CD2 LEU A 626 58.680 0.441 18.639 1.00 17.72 4008 N LEU A 627 57.659 −4.144 21.467 1.00 16.19 4009 CA LEU A 627 58.113 −5.513 21.759 1.00 15.53 4010 C LEU A 627 57.363 −6.526 20.913 1.00 16.98 4011 O LEU A 627 57.855 −7.640 20.681 1.00 17.15 4012 CB LEU A 627 57.921 −5.793 23.258 1.00 13.38 4013 CG LEU A 627 58.686 −4.849 24.212 1.00 15.02 4014 CD1 LEU A 627 58.414 −5.232 25.681 1.00 15.03 4015 CD2 LEU A 627 60.170 −4.930 23.934 1.00 14.76 4016 N GLY A 628 56.185 −6.119 20.421 1.00 17.12 4017 CA GLY A 628 55.382 −6.956 19.534 1.00 18.12 4018 C GLY A 628 54.439 −7.946 20.204 1.00 17.72 4019 O GLY A 628 54.669 −8.439 21.306 1.00 16.57 4020 N LYS A 629 53.318 −8.265 19.560 1.00 18.93 4021 CA LYS A 629 52.277 −9.137 20.075 1.00 20.91 4022 C LYS A 629 52.713 −10.539 20.453 1.00 19.69 4023 O LYS A 629 52.362 −11.008 21.533 1.00 16.07 4024 CB LYS A 629 51.156 −9.305 19.012 1.00 25.01 4025 CG LYS A 629 49.955 −8.430 19.255 1.00 30.66 4026 CD LYS A 629 48.648 −9.053 18.751 1.00 34.60 4027 CE LYS A 629 48.662 −9.270 17.249 1.00 36.35 4028 NZ LYS A 629 47.246 −9.312 16.726 1.00 39.65 4029 N ASP A 630 53.433 −11.217 19.563 1.00 19.67 4030 CA ASP A 630 53.949 −12.557 19.788 1.00 21.78 4031 C ASP A 630 54.931 −12.616 20.960 1.00 19.85 4032 O ASP A 630 54.849 −13.490 21.817 1.00 18.70 4033 CB ASP A 630 54.660 −13.041 18.517 1.00 26.04 4034 CG ASP A 630 53.695 −13.269 17.360 1.00 31.74 4035 OD1 ASP A 630 54.169 −13.303 16.193 1.00 34.75 4036 OD2 ASP A 630 52.469 −13.434 17.529 1.00 33.72 4037 N THR A 631 55.845 −11.675 21.097 1.00 18.89 4038 CA THR A 631 56.697 −11.571 22.286 1.00 17.67 4039 C THR A 631 55.928 −11.360 23.584 1.00 17.16 4040 O THR A 631 56.197 −12.037 24.596 1.00 17.74 4041 CB THR A 631 57.728 −10.455 22.062 1.00 16.84 4042 OG1 THR A 631 58.509 −10.815 20.895 1.00 16.86 4043 CG2 THR A 631 58.658 −10.288 23.259 1.00 14.40 4044 N MET A 632 54.947 −10.471 23.613 1.00 15.74 4045 CA MET A 632 54.128 −10.195 24.787 1.00 16.10 4046 C MET A 632 53.304 −11.399 25.193 1.00 17.20 4047 O MET A 632 53.196 −11.659 26.389 1.00 16.17 4048 CB MET A 632 53.256 −8.950 24.696 1.00 14.99 4049 CG MET A 632 53.997 −7.596 24.713 1.00 13.86 4050 SD MET A 632 55.378 −7.434 25.863 1.00 14.63 4051 CE MET A 632 54.506 −7.782 27.400 1.00 15.56 4052 N ALA A 633 52.764 −12.173 24.245 1.00 17.51 4053 CA ALA A 633 52.008 −13.370 24.597 1.00 17.78 4054 C ALA A 633 52.902 −14.414 25.286 1.00 18.00 4055 O ALA A 633 52.463 −15.073 26.245 1.00 15.84 4056 CB ALA A 633 51.391 −13.971 23.328 1.00 16.07 4057 N LYS A 634 54.135 −14.550 24.791 1.00 18.45 4058 CA LYS A 634 55.101 −15.503 25.368 1.00 19.92 4059 C LYS A 634 55.571 −15.082 26.757 1.00 19.10 4060 O LYS A 634 55.753 −15.910 27.661 1.00 16.95 4061 CB LYS A 634 56.365 −15.667 24.495 1.00 21.98 4062 CG LYS A 634 56.109 −16.327 23.139 1.00 25.49 4063 CD LYS A 634 57.432 −16.789 22.524 1.00 27.52 4064 CE LYS A 634 57.239 −17.490 21.173 1.00 27.96 4065 NZ LYS A 634 58.537 −17.479 20.413 1.00 29.38 4066 N ILE A 635 55.768 −13.775 26.941 1.00 17.02 4067 CA ILE A 635 56.142 −13.264 28.263 1.00 17.04 4068 C ILE A 635 54.985 −13.581 29.221 1.00 18.26 4069 O ILE A 635 55.242 −14.096 30.321 1.00 16.99 4070 CB ILE A 635 56.444 −11.752 28.267 1.00 18.88 4071 CG1 ILE A 635 57.787 −11.462 27.535 1.00 18.51 4072 CG2 ILE A 635 56.370 −11.171 29.670 1.00 15.03 4073 CD1 ILE A 635 58.004 −9.955 27.358 1.00 18.80 4074 N SER A 636 53.742 −13.211 28.818 1.00 16.75 4075 CA SER A 636 52.587 −13.505 29.684 1.00 16.38 4076 C SER A 636 52.396 −14.985 29.963 1.00 17.44 4077 O SER A 636 52.268 −15.366 31.134 1.00 15.83 4078 CB SER A 636 51.327 −12.920 29.022 1.00 17.93 4079 OG SER A 636 50.145 −13.262 29.716 1.00 18.44 4080 N ASN A 637 52.473 −15.869 28.956 1.00 18.57 4081 CA ASN A 637 52.375 −17.314 29.219 1.00 20.52 4082 C ASN A 637 53.492 −17.878 30.092 1.00 21.51 4083 O ASN A 637 53.154 −18.683 30.984 1.00 22.24 4084 CB ASN A 637 52.291 −18.099 27.902 1.00 19.88 4085 CG ASN A 637 51.013 −17.754 27.145 1.00 21.97 4086 OD1 ASN A 637 50.142 −17.046 27.666 1.00 23.68 4087 ND2 ASN A 637 50.868 −18.237 25.912 1.00 21.76 4088 N GLU A 638 54.752 −17.482 29.901 1.00 19.30 4089 CA GLU A 638 55.825 −17.997 30.751 1.00 21.15 4090 C GLU A 638 55.668 −17.545 32.199 1.00 19.63 4091 O GLU A 638 55.839 −18.358 33.122 1.00 19.31 4092 CB GLU A 638 57.218 −17.580 30.253 1.00 21.35 4093 CG GLU A 638 57.655 −18.382 29.023 1.00 22.98 4094 CD GLU A 638 59.094 −18.201 28.573 1.00 24.51 4095 OE1 GLU A 638 59.324 −18.637 27.404 1.00 24.01 4096 OE2 GLU A 638 59.978 −17.673 29.315 1.00 22.90 4097 N LEU A 639 55.428 −16.257 32.402 1.00 18.27 4098 CA LEU A 639 55.291 −15.771 33.784 1.00 19.11 4099 C LEU A 639 54.017 −16.268 34.422 1.00 19.62 4100 O LEU A 639 54.073 −16.629 35.613 1.00 19.57 4101 CB LEU A 639 55.454 −14.237 33.905 1.00 17.12 4102 CG LEU A 639 56.786 −13.720 33.342 1.00 17.07 4103 CD1 LEU A 639 56.903 −12.195 33.297 1.00 15.55 4104 CD2 LEU A 639 57.975 −14.331 34.093 1.00 16.23 4105 N HIS A 640 52.879 −16.404 33.716 1.00 19.06 4106 CA HIS A 640 51.679 −16.908 34.394 1.00 20.34 4107 C HIS A 640 51.739 −18.383 34.784 1.00 22.10 4108 O HIS A 640 50.969 −18.816 35.671 1.00 21.35 4109 CB HIS A 640 50.420 −16.629 33.582 1.00 19.39 4110 CG HIS A 640 50.102 −15.160 33.517 1.00 20.54 4111 ND1 HIS A 640 50.217 −14.293 34.601 1.00 19.70 4112 CD2 HIS A 640 49.610 −14.433 32.483 1.00 18.57 4113 CE1 HIS A 640 49.752 −13.097 34.246 1.00 18.71 4114 NE2 HIS A 640 49.412 −13.172 32.965 1.00 19.82 4115 N ALA A 641 52.612 −19.173 34.200 1.00 23.98 4116 CA ALA A 641 52.801 −20.579 34.579 1.00 26.49 4117 C ALA A 641 53.598 −20.615 35.882 1.00 27.89 4118 O ALA A 641 53.510 −21.587 36.628 1.00 31.74 4119 CB ALA A 641 53.605 −21.327 33.512 1.00 26.50 4120 N ILE A 642 54.437 −19.626 36.174 1.00 28.13 4121 CA ILE A 642 55.107 −19.555 37.476 1.00 29.40 4122 C ILE A 642 54.093 −19.073 38.530 1.00 28.86 4123 O ILE A 642 53.932 −19.665 39.596 1.00 26.64 4124 CB ILE A 642 56.310 −18.608 37.450 1.00 29.90 4125 CG1 ILE A 642 57.312 −18.997 36.344 1.00 30.38 4126 CG2 ILE A 642 57.009 −18.615 38.817 1.00 30.02 4127 CD1 ILE A 642 58.394 −17.943 36.170 1.00 30.48 4128 N ASN A 643 53.361 −17.993 38.188 1.00 26.34 4129 CA ASN A 643 52.345 −17.452 39.112 1.00 23.82 4130 C ASN A 643 51.282 −16.700 38.316 1.00 24.17 4131 O ASN A 643 51.544 −15.628 37.774 1.00 21.45 4132 CB ASN A 643 53.051 −16.543 40.122 1.00 22.05 4133 CG ASN A 643 52.079 −15.861 41.083 1.00 23.41 4134 OD1 ASN A 643 50.871 −16.089 41.037 1.00 21.01 4135 ND2 ASN A 643 52.555 −15.009 41.966 1.00 22.58 4136 N PRO A 644 50.049 −17.213 38.277 1.00 23.33 4137 CA PRO A 644 48.956 −16.613 37.531 1.00 22.06 4138 C PRO A 644 48.572 −15.222 37.983 1.00 19.69 4139 O PRO A 644 47.936 −14.499 37.220 1.00 20.72 4140 CB PRO A 644 47.77 −17.582 37.713 1.00 23.07 4141 CG PRO A 644 48.101 −18.344 38.959 1.00 24.32 4142 CD PRO A 644 49.621 −18.473 38.945 1.00 23.67 4143 N GLY A 645 48.892 −14.797 39.190 1.00 18.01 4144 CA GLY A 645 48.637 −13.494 39.741 1.00 17.70 4145 C GLY A 645 49.592 −12.380 39.283 1.00 19.60 4146 O GLY A 645 49.390 −11.193 39.628 1.00 15.48 4147 N ILE A 646 50.660 −12.723 38.538 1.00 18.09 4148 CA ILE A 646 51.643 −11.732 38.106 1.00 17.16 4149 C ILE A 646 50.986 −10.704 37.203 1.00 16.23 4150 O ILE A 646 50.260 −11.076 36.307 1.00 17.07 4151 CB ILE A 646 52.885 −12.409 37.477 1.00 17.81 4152 CG1 ILE A 646 53.818 −12.981 38.569 1.00 18.48 4153 CG2 ILE A 646 53.723 −11.434 36.653 1.00 17.45 4154 CD1 ILE A 646 54.986 −13.812 38.061 1.00 16.75 4155 N VAL A 647 51.202 −9.403 37.398 1.00 16.03 4156 CA VAL A 647 50.549 −8.329 36.668 1.00 15.29 4157 C VAL A 647 51.490 −7.688 35.644 1.00 16.91 4158 O VAL A 647 52.608 −7.229 35.981 1.00 14.67 4159 CB VAL A 647 50.020 −7.276 37.651 1.00 16.53 4160 CG1 VAL A 647 49.281 −6.165 36.945 1.00 15.28 4161 CG2 VAL A 647 49.094 −7.913 38.727 1.00 15.02 4162 N LEU A 648 51.048 −7.688 34.392 1.00 13.55 4163 CA LEU A 648 51.862 −7.214 33.256 1.00 16.97 4164 C LEU A 648 51.149 −6.179 32.396 1.00 17.87 4165 O LEU A 648 49.993 −6.422 32.031 1.00 18.62 4166 CB LEU A 648 52.123 −8.454 32.390 1.00 14.99 4167 CG LEU A 648 52.778 −9.673 33.034 1.00 14.65 4168 CD1 LEU A 648 52.716 −10.926 32.153 1.00 12.97 4169 CD2 LEU A 648 54.247 −9.321 33.383 1.00 12.67 4170 N TYR A 649 51.744 −5.012 32.124 1.00 17.59 4171 CA TYR A 649 51.053 −3.961 31.359 1.00 17.71 4172 C TYR A 649 52.086 −3.025 30.737 1.00 18.28 4173 O TYR A 649 53.272 −3.151 31.086 1.00 18.59 4174 CB TYR A 649 50.082 −3.164 32.269 1.00 14.25 4175 CG TYR A 649 50.752 −2.654 33.527 1.00 13.60 4176 CD1 TYR A 649 50.833 −3.456 34.665 1.00 14.53 4177 CD2 TYR A 649 51.240 −1.358 33.610 1.00 11.51 4178 CE1 TYR A 649 51.501 −3.023 35.819 1.00 13.05 4179 CE2 TYR A 649 51.869 −0.891 34.758 1.00 13.13 4180 CZ TYR A 649 52.001 −1.743 35.853 1.00 14.34 4181 OH TYR A 649 52.639 −1.254 36.972 1.00 11.99 4182 N GLY A 650 51.670 −2.046 29.915 1.00 18.09 4183 CA GLY A 650 52.684 −1.112 29.378 1.00 16.66 4184 C GLY A 650 52.088 −0.094 28.439 1.00 17.73 4185 O GLY A 650 50.851 −0.034 28.270 1.00 16.48 4186 N GLU A 651 52.922 0.800 27.876 1.00 17.53 4187 CA GLU A 651 52.431 1.880 27.026 1.00 17.39 4188 C GLU A 651 52.077 1.368 25.620 1.00 17.53 4189 O GLU A 651 52.976 0.899 24.910 1.00 19.12 4190 CB GLU A 651 53.546 2.926 26.950 1.00 19.60 4191 CG GLU A 651 53.976 3.596 28.238 1.00 20.41 4192 CD GLU A 651 55.141 4.573 28.068 1.00 22.59 4193 OE1 GLU A 651 56.242 4.141 27.636 1.00 18.94 4194 OE2 GLU A 651 54.935 5.780 28.390 1.00 20.69 4195 N PRO A 652 50.856 1.556 25.122 1.00 17.10 4196 CA PRO A 652 50.515 1.043 23.784 1.00 18.38 4197 C PRO A 652 50.940 1.945 22.648 1.00 18.28 4198 O PRO A 652 50.125 2.221 21.773 1.00 19.43 4199 CB PRO A 652 48.957 0.908 23.883 1.00 17.61 4200 CG PRO A 652 48.591 2.087 24.748 1.00 16.44 4201 CD PRO A 652 49.695 2.112 25.852 1.00 15.52 4202 N TRP A 653 52.098 2.594 22.614 1.00 18.69 4203 CA TRP A 653 52.549 3.503 21.554 1.00 18.43 4204 C TRP A 653 54.065 3.398 21.359 1.00 17.97 4205 O TRP A 653 54.779 2.764 22.137 1.00 15.71 4206 CB TRP A 653 52.091 4.950 21.814 1.00 19.02 4207 CG TRP A 653 52.439 5.531 23.150 1.00 18.75 4208 CD1 TRP A 653 53.669 5.991 23.523 1.00 20.11 4209 CD2 TRP A 653 51.603 5.706 24.308 1.00 20.38 4210 NE1 TRP A 653 53.655 6.453 24.824 1.00 20.51 4211 CE2 TRP A 653 52.378 6.290 25.318 1.00 20.60 4212 CE3 TRP A 653 50.242 5.446 24.554 1.00 19.16 4213 CZ2 TRP A 653 51.869 6.584 26.595 1.00 22.37 4214 CZ3 TRP A 653 49.738 5.760 25.813 1.00 19.76 4215 CH2 TRP A 653 50.542 6.323 26.813 1.00 20.77 4216 N THR A 654 54.658 4.006 20.338 1.00 17.06 4217 CA THR A 654 56.072 4.010 20.058 1.00 18.41 4218 C THR A 654 56.620 5.431 20.270 1.00 19.84 4219 O THR A 654 55.835 6.339 20.572 1.00 20.60 4220 CB THR A 654 56.438 3.591 18.608 1.00 19.02 4221 OG1 THR A 654 56.079 4.691 17.734 1.00 18.49 4222 CG2 THR A 654 55.687 2.359 18.174 1.00 16.83 4223 N GLY A 655 57.916 5.601 20.196 1.00 21.18 4224 CA GLY A 655 58.633 6.858 20.389 1.00 21.26 4225 C GLY A 655 58.929 7.605 19.077 1.00 24.38 4226 O GLY A 655 58.912 8.849 19.015 1.00 24.84 4227 N GLY A 656 59.178 6.896 18.002 1.00 22.39 4228 CA GLY A 656 59.338 7.387 16.58 1.00 24.45 4229 C GLY A 656 58.840 6.337 15.661 1.00 25.22 4230 O GLY A 656 58.050 5.459 16.055 1.00 25.29 4231 N THR A 657 59.280 6.365 14.403 1.00 23.11 4232 CA THR A 657 58.848 5.425 13.380 1.00 23.56 4233 C THR A 657 59.546 4.082 13.588 1.00 22.19 4234 O THR A 657 60.759 4.098 13.820 1.00 20.73 4235 CB THR A 657 59.256 5.972 11.983 1.00 26.11 4236 OG1 THR A 657 58.698 7.292 11.803 1.00 27.58 4237 CG2 THR A 657 58.669 5.066 10.912 1.00 26.30 4238 N SER A 658 58.846 2.963 13.574 1.00 22.05 4239 CA SER A 658 59.408 1.688 13.981 1.00 22.49 4240 C SER A 658 59.740 0.805 12.779 1.00 23.91 4241 O SER A 658 58.952 0.966 11.879 1.00 21.76 4242 CB SER A 658 58.435 0.890 14.874 1.00 22.19 4243 OG SER A 658 59.035 −0.398 15.133 1.00 20.61 4244 N GLY A 659 60.747 −0.101 12.852 1.00 22.44 4245 CA GLY A 659 60.886 −1.041 11.765 1.00 22.70 4246 C GLY A 659 59.939 −2.211 11.917 1.00 24.64 4247 O GLY A 659 59.836 −3.016 10.967 1.00 25.07 4248 N LEU A 660 59.245 −2.383 13.049 1.00 22.82 4249 CA LEU A 660 58.349 −3.534 13.163 1.00 22.64 4250 C LEU A 660 57.049 −3.271 12.408 1.00 24.58 4251 O LEU A 660 56.462 −2.191 12.541 1.00 23.39 4252 CB LEU A 660 58.032 −3.798 14.656 1.00 21.87 4253 CG LEU A 660 57.221 −5.073 14.921 1.00 21.46 4254 CD1 LEU A 660 58.005 −6.333 14.553 1.00 21.53 4255 CD2 LEU A 660 56.796 −5.118 16.387 1.00 22.01 4256 N SER A 661 56.498 −4.299 11.768 1.00 28.28 4257 CA SER A 661 55.249 −4.110 11.039 1.00 31.06 4258 C SER A 661 54.123 −3.721 11.988 1.00 31.92 4259 O SER A 661 53.977 −4.115 13.149 1.00 30.73 4260 CB SER A 661 54.841 −5.369 10.278 1.00 33.28 4261 OG SER A 661 54.406 −6.282 11.303 1.00 38.97 4262 N SER A 662 53.207 −2.944 11.425 1.00 31.42 4263 CA SER A 662 52.040 −2.489 12.164 1.00 31.08 4264 C SER A 662 51.177 −3.592 12.719 1.00 30.70 4265 O SER A 662 50.577 −3.441 13.808 1.00 29.15 4266 CB SER A 662 51.250 −1.605 11.179 1.00 33.72 4267 OG SER A 662 50.239 −0.982 11.936 1.00 37.74 4268 N ASP A 663 51.069 −4.738 12.047 1.00 29.07 4269 CA ASP A 663 50.244 −5.830 12.522 1.00 30.96 4270 C ASP A 663 50.781 −6.442 13.814 1.00 27.66 4271 O ASP A 663 50.053 −7.210 14.429 1.00 24.98 4272 CB ASP A 663 50.219 −6.998 11.510 1.00 37.98 4273 CG ASP A 663 50.022 −6.418 10.118 1.00 43.25 4274 OD1 ASP A 663 51.041 −6.067 9.479 1.00 46.25 4275 OD2 ASP A 63 48.826 −6.288 9.774 1.00 46.03 4276 N GLN A 664 52.066 −6.234 14.108 1.00 22.67 4277 CA GLN A 664 52.601 −6.838 15.333 1.00 23.37 4278 C GLN A 664 52.675 −5.789 16.432 1.00 22.24 4279 O GLN A 664 52.822 −6.210 17.585 1.00 19.91 4280 CB GLN A 664 53.947 −7.514 15.015 1.00 23.40 4281 CG GLN A 664 53.799 −8.961 14.521 1.00 24.74 4282 CD GLN A 664 53.177 −9.871 16.593 1.00 25.49 4283 OE1 GLN A 664 53.749 −9.992 16.703 1.00 24.23 4284 NE2 GLN A 664 52.036 −10.506 15.305 1.00 23.12 4285 N LEU A 665 52.600 −4.486 16.125 1.00 19.96 4286 CA LEU A 665 52.740 −3.486 17.200 1.00 19.39 4287 C LEU A 665 51.651 −3.648 18.238 1.00 18.71 4288 O LEU A 665 50.488 −3.843 17.884 1.00 17.87 4289 CB LEU A 665 52.765 −2.046 16.656 1.00 20.03 4290 CG LEU A 665 53.973 −1.662 15.786 1.00 21.89 4291 CD1 LEU A 665 53.709 −0.411 14.951 1.00 20.88 4292 CD2 LEU A 665 55.207 −1.501 16.668 1.00 22.05 4293 N VAL A 666 51.929 −3.519 19.533 1.00 18.78 4294 CA VAL A 666 50.885 −3.678 20.558 1.00 18.52 4295 C VAL A 666 50.237 −2.321 20.883 1.00 19.69 4296 O VAL A 666 50.466 −1.789 21.955 1.00 17.22 4297 CB VAL A 666 51.359 −4.354 21.835 1.00 16.96 4298 CG1 VAL A 666 50.206 −4.834 22.723 1.00 19.29 4299 CG2 VAL A 666 52.295 −5.532 21.529 1.00 14.78 4300 N THR A 667 49.290 −1.919 20.033 1.00 20.48 4301 CA THR A 667 48.502 −0.702 20.179 1.00 20.14 4302 C THR A 667 47.197 −1.024 20.902 1.00 18.13 4303 O THR A 667 46.985 −2.227 21.117 1.00 16.98 4304 CB THR A 667 48.269 −0.014 18.814 1.00 21.55 4305 OG1 THR A 667 47.843 −1.044 17.925 1.00 20.10 4306 CG2 THR A 667 49.597 0.611 18.281 1.00 21.18 4307 N LYS A 668 46.331 −0.058 21.255 1.00 16.86 4308 CA LYS A 668 45.140 −0.468 22.022 1.00 18.52 4309 C LYS A 668 44.229 −1.401 21.234 1.00 19.25 4310 O LYS A 668 43.936 −1.077 20.104 1.00 15.25 4311 CB LYS A 668 44.277 0.724 22.546 1.00 17.82 4312 CG LYS A 668 45.148 1.580 23.472 1.00 19.27 4313 CD LYS A 668 44.324 2.507 24.357 1.00 22.35 4314 CE LYS A 668 43.581 3.587 23.574 1.00 22.93 4315 NZ LYS A 668 44.581 4.231 22.654 1.00 24.34 4316 N GLY A 669 43.759 −2.439 21.897 1.00 20.04 4317 CA GLY A 669 42.938 −3.451 21.239 1.00 20.82 4318 C GLY A 669 43.782 −4.704 20.955 1.00 21.65 4319 O GLY A 669 43.213 −5.800 20.927 1.00 21.36 4320 N GLN A 670 45.088 −4.594 20.719 1.00 20.53 4321 CA GLN A 670 45.919 −5.759 20.428 1.00 21.35 4322 C GLN A 670 46.297 −6.586 21.642 1.00 20.10 4323 O GLN A 670 46.749 −7.720 21.456 1.00 19.47 4324 CB GLN A 670 47.247 −5.387 19.714 1.00 21.19 4325 CG GLN A 670 46.970 −4.705 18.368 1.00 27.47 4326 CD GLN A 670 46.169 −5.614 17.439 1.00 31.69 4327 OE1 GLN A 670 46.616 −6.684 17.021 1.00 32.50 4328 NE2 GLN A 670 44.937 −5.233 17.073 1.00 34.39 4329 N GLN A 671 45.972 −6.145 22.858 1.00 19.44 4330 CA GLN A 671 46.228 −6.920 24.059 1.00 19.31 4331 C GLN A 671 45.108 −7.890 24.371 1.00 19.04 4332 O GLN A 671 45.181 −8.640 25.368 1.00 19.01 4333 CB GLN A 671 46.423 −5.943 25.252 1.00 18.95 4334 CG GLN A 671 45.140 −5.479 25.924 1.00 18.55 4335 CD GLN A 671 44.177 −4.651 25.083 1.00 18.72 4336 OE1 GLN A 671 42.932 −4.761 25.238 1.00 19.28 4337 NE2 GLN A 671 44.667 −3.817 24.177 1.00 15.65 4338 N LYS A 672 43.957 −7.772 23.698 1.00 17.47 4339 CA LYS A 672 42.772 −8.535 24.053 1.00 18.28 4340 C LYS A 672 43.062 −10.006 24.247 1.00 17.84 4341 O LYS A 672 43.624 −10.599 23.339 1.00 17.28 4342 CB LYS A 672 41.622 −8.448 23.030 1.00 21.13 4343 CG LYS A 672 40.888 −7.108 22.987 1.00 22.83 4344 CD LYS A 672 39.854 −7.147 21.817 1.00 27.44 4345 CE LYS A 672 38.826 −6.074 22.145 1.00 30.81 4346 NZ LYS A 672 37.962 −5.616 21.015 1.00 33.27 4347 N GLY A 673 42.644 −10.575 25.384 1.00 17.84 4348 CA GLY A 673 42.889 −11.973 25.692 1.00 16.83 4349 C GLY A 673 44.324 −12.396 25.938 1.00 17.57 4350 O GLY A 673 44.584 −13.612 26.132 1.00 16.05 4351 N LEU A 674 45.337 −11.535 26.003 1.00 16.87 4352 CA LEU A 674 46.707 −12.002 26.224 1.00 17.22 4353 C LEU A 674 47.121 −12.089 27.692 1.00 18.69 4354 O LEU A 674 48.214 −12.614 27.992 1.00 16.27 4355 CB LEU A 674 47.668 −11.070 25.482 1.00 16.47 4356 CG LEU A 674 47.491 −10.955 23.957 1.00 17.85 4357 CD1 LEU A 674 48.601 −10.153 23.292 1.00 17.96 4358 CD2 LEU A 674 47.402 −12.356 23.376 1.00 17.89 4359 N GLY A 675 46.351 −11.448 28.580 1.00 17.76 4360 CA GLY A 675 46.690 −11.447 29.992 1.00 18.55 4361 C GLY A 675 47.533 −10.238 30.385 1.00 18.93 4362 O GLY A 675 48.418 −10.331 31.244 1.00 17.89 4363 N ILE A 676 47.527 −9.199 29.566 1.00 18.34 4364 CA ILE A 676 48.279 −7.984 29.777 1.00 16.64 4365 C ILE A 676 47.341 −6.773 29.627 1.00 17.75 4366 O ILE A 676 46.311 −6.893 28.941 1.00 16.31 4367 CB ILE A 676 49.479 −7.831 28.825 1.00 19.70 4368 CG1 ILE A 676 49.028 −7.552 27.392 1.00 20.32 4369 CG2 ILE A 676 50.426 −9.050 28.832 1.00 17.85 4370 CD1 ILE A 676 50.167 −7.324 26.394 1.00 17.85 4371 N GLY A 677 47.751 −5.639 30.156 1.00 13.65 4372 CA GLY A 677 47.021 −4.394 30.070 1.00 15.81 4373 C GLY A 677 47.769 −3.254 29.403 1.00 16.01 4374 O GLY A 677 48.991 −3.301 29.151 1.00 16.11 4375 N VAL A 678 47.038 −2.172 29.079 1.00 15.57 4376 CA VAL A 678 47.638 −1.027 28.427 1.00 15.53 4377 C VAL A 678 47.199 0.251 29.119 1.00 16.70 4378 O VAL A 678 46.014 0.364 29.518 1.00 18.08 4379 CB VAL A 678 47.310 −0.949 26.919 1.00 14.79 4380 CG1 VAL A 678 47.819 −2.120 26.065 1.00 16.01 4381 CG2 VAL A 678 45.761 −0.920 26.704 1.00 15.88 4382 N PHE A 679 48.111 1.185 29.240 1.00 12.93 4383 CA PHE A 679 47.799 2.494 29.790 1.00 13.80 4384 C PHE A 679 46.705 3.036 28.866 1.00 16.99 4385 O PHE A 679 46.830 3.061 27.626 1.00 16.58 4386 CB PHE A 679 49.075 3.354 29.813 1.00 15.10 4387 CG PHE A 679 49.992 3.064 30.997 1.00 16.37 4388 CD1 PHE A 679 51.234 2.485 30.823 1.00 17.10 4389 CD2 PHE A 679 49.591 3.420 32.282 1.00 15.14 4390 CE1 PHE A 679 52.097 2.258 31.903 1.00 17.80 4391 CE2 PHE A 679 50.451 3.191 33.364 1.00 17.84 4392 CZ PHE A 679 51.687 2.594 33.195 1.00 16.20 4393 N ASN A 680 45.614 3.469 29.502 1.00 17.15 4394 CA ASN A 680 44.468 3.996 28.753 1.00 16.69 4395 C ASN A 680 44.612 5.491 28.529 1.00 16.69 4396 O ASN A 680 44.157 6.287 29.363 1.00 15.66 4397 CB ASN A 680 43.205 3.658 29.584 1.00 15.17 4398 CG ASN A 680 41.905 4.021 28.891 1.00 16.39 4399 OD1 ASN A 680 40.786 3.672 29.326 1.00 19.69 4400 ND2 ASN A 680 41.946 4.799 27.835 1.00 13.35 4401 N ASP A 681 45.204 5.905 27.392 1.00 15.34 4402 CA ASP A 681 45.322 7.314 27.098 1.00 17.64 4403 C ASP A 681 43.983 7.925 26.684 1.00 15.96 4404 O ASP A 681 43.930 9.146 26.750 1.00 18.29 4405 CB ASP A 681 46.434 7.675 26.088 1.00 16.68 4406 CG ASP A 681 46.314 6.929 24.779 1.00 20.08 4407 OD1 ASP A 681 45.917 5.745 24.708 1.00 18.82 4408 OD2 ASP A 681 46.590 7.570 23.728 1.00 21.03 4409 N ASN A 682 42.939 7.183 26.388 1.00 16.19 4410 CA ASN A 682 41.626 7.732 26.064 1.00 16.30 4411 C ASN A 682 41.008 8.391 27.314 1.00 17.28 4412 O ASN A 682 40.543 9.554 27.320 1.00 16.98 4413 CB ASN A 682 40.706 6.629 25.496 1.00 15.40 4414 CG ASN A 682 41.010 6.205 24.062 1.00 17.13 4415 OD1 ASN A 682 41.866 6.815 23.416 1.00 16.74 4416 ND2 ASN A 682 40.350 5.175 23.511 1.00 15.15 4417 N ILE A 683 41.032 7.677 28.454 1.00 16.35 4418 CA ILE A 683 40.470 8.220 29.694 1.00 16.07 4419 C ILE A 683 41.284 9.380 30.251 1.00 17.30 4420 O ILE A 683 40.836 10.455 30.737 1.00 17.55 4421 CB ILE A 683 40.228 7.122 30.748 1.00 16.73 4422 CG1 ILE A 683 39.118 7.666 31.683 1.00 17.76 4423 CG2 ILE A 683 41.474 6.693 31.535 1.00 13.77 4424 CD1 ILE A 683 38.930 6.930 32.986 1.00 18.13 4425 N ARG A 684 42.600 9.261 30.064 1.00 15.73 4426 CA ARG A 684 43.514 10.306 30.488 1.00 16.66 4427 C ARG A 684 43.207 11.587 29.736 1.00 15.87 4428 O ARG A 684 43.115 12.677 30.317 1.00 16.71 4429 CB ARG A 684 44.976 9.857 30.262 1.00 18.05 4430 CG ARG A 684 45.952 10.905 30.788 1.00 20.35 4431 CD ARG A 684 47.222 11.054 30.003 1.00 26.33 4432 NE ARG A 684 47.113 11.061 28.560 1.00 30.02 4433 CZ ARG A 684 48.001 10.589 27.682 1.00 32.36 4434 NH1 ARG A 684 49.205 10.033 27.964 1.00 33.59 4435 NH2 ARG A 684 47.644 10.673 26.404 1.00 33.28 4436 N ASN A 685 43.193 11.515 28.410 1.00 15.54 4437 CA ASN A 685 42.944 12.721 27.596 1.00 17.75 4438 C ASN A 685 41.554 13.294 27.914 1.00 16.60 4439 O ASN A 685 41.377 14.510 27.960 1.00 16.32 4440 CB ASN A 685 43.101 12.404 26.078 1.00 15.79 4441 CG ASN A 685 44.559 12.204 25.670 1.00 17.29 4442 OD1 ASN A 685 45.564 12.731 26.189 1.00 15.27 4443 ND2 ASN A 685 44.757 11.357 24.661 1.00 18.75 4444 N GLY A 686 40.581 12.454 28.172 1.00 16.82 4445 CA GLY A 686 39.208 12.841 28.482 1.00 18.79 4446 C GLY A 686 39.085 13.538 29.825 1.00 18.90 4447 O GLY A 686 38.321 14.506 29.982 1.00 18.03 4448 N LEU A 687 39.870 13.071 30.804 1.00 18.75 4449 CA LEU A 687 39.858 13.683 32.131 1.00 17.87 4450 C LEU A 687 40.445 15.084 32.155 1.00 19.56 4451 O LEU A 687 39.835 15.949 32.801 1.00 18.35 4452 CB LEU A 687 40.553 12.740 33.143 1.00 17.50 4453 CG LEU A 687 39.691 11.524 33.514 1.00 16.49 4454 CD1 LEU A 687 40.525 10.497 34.266 1.00 15.82 4455 CD2 LEU A 687 38.459 11.960 34.349 1.00 17.74 4456 N ASP A 688 41.590 15.386 31.529 1.00 19.00 4457 CA ASP A 688 42.114 16.743 31.606 1.00 19.09 4458 C ASP A 688 42.632 17.315 30.289 1.00 18.61 4459 O ASP A 688 43.299 18.348 30.374 1.00 17.40 4460 CB ASP A 688 43.247 16.843 32.624 1.00 21.76 4461 CG ASP A 688 44.491 16.033 32.362 1.00 25.24 4462 OD1 ASP A 688 44.577 15.205 31.412 1.00 26.02 4463 OD2 ASP A 688 45.452 16.200 33.160 1.00 24.89 4464 N GLY A 689 42.237 16.788 29.143 1.00 19.33 4465 CA GLY A 689 42.679 17.411 27.872 1.00 20.12 4466 C GLY A 689 43.852 16.650 27.244 1.00 21.08 4467 O GLY A 689 44.631 15.975 27.940 1.00 18.25 4468 N ASN A 690 43.957 16.778 25.912 1.00 20.39 4469 CA ASN A 690 45.008 16.103 25.159 1.00 18.52 4470 C ASN A 690 46.382 16.400 25.702 1.00 18.62 4471 O ASN A 690 46.767 17.560 25.942 1.00 18.86 4472 CB ASN A 690 44.883 16.503 23.659 1.00 20.87 4473 CG ASN A 690 45.899 15.668 22.877 1.00 22.43 4474 OD1 ASN A 690 47.036 16.114 22.664 1.00 22.38 4475 ND2 ASN A 690 45.472 14.460 22.513 1.00 21.21 4476 N VAL A 691 47.256 15.408 25.828 1.00 17.79 4477 CA VAL A 691 48.582 15.528 26.410 1.00 20.26 4478 C VAL A 691 49.536 16.419 25.616 1.00 20.63 4479 O VAL A 691 50.503 16.940 26.182 1.00 19.98 4480 CB VAL A 691 49.204 14.114 26.594 1.00 21.95 4481 CG1 VAL A 691 49.485 13.451 25.233 1.00 19.94 4482 CG2 VAL A 691 50.487 14.150 27.404 1.00 21.70 4483 N PHE A 692 49.287 16.668 24.331 1.00 19.63 4484 CA PHE A 692 50.187 17.533 23.544 1.00 20.10 4485 C PHE A 692 49.799 19.008 23.561 1.00 18.56 4486 O PHE A 692 50.399 19.821 22.869 1.00 18.61 4487 CB PHE A 692 50.238 17.053 22.090 1.00 18.53 4488 CG PHE A 692 50.859 15.694 21.969 1.00 21.54 4489 CD1 PHE A 692 50.085 14.538 21.907 1.00 20.75 4490 CD2 PHE A 692 52.245 15.579 21.964 1.00 21.43 4491 CE1 PHE A 692 50.723 13.309 21.812 1.00 21.57 4492 CE2 PHE A 692 52.865 14.348 21.891 1.00 21.34 4493 CZ PHE A 692 52.097 13.205 21.793 1.00 21.14 4494 N ASP A 693 48.780 19.382 24.314 1.00 19.75 4495 CA ASP A 693 48.307 20.760 24.442 1.00 18.18 4496 C ASP A 693 48.252 21.124 25.925 1.00 20.25 4497 O ASP A 693 47.300 20.850 26.671 1.00 15.97 4498 CB ASP A 693 46.932 20.849 23.734 1.00 20.28 4499 CG ASP A 693 46.336 22.240 23.779 1.00 22.51 4500 OD1 ASP A 693 45.186 22.441 23.333 1.00 24.25 4501 OD2 ASP A 693 47.013 23.154 24.306 1.00 23.36 4502 N LYS A 694 49.301 21.803 26.426 1.00 22.37 4503 CA LYS A 694 49.397 22.197 27.836 1.00 26.78 4504 C LYS A 694 48.227 23.020 28.342 1.00 25.75 4505 O LYS A 694 47.839 22.882 29.508 1.00 26.28 4506 CB LYS A 694 50.739 22.873 28.133 1.00 30.68 4507 CG LYS A 694 50.740 24.392 28.225 1.00 35.67 4508 CD LYS A 694 52.036 24.960 28.789 1.00 39.09 4509 CE LYS A 694 52.086 26.494 28.763 1.00 41.48 4510 NZ LYS A 694 50.861 27.195 29.329 1.00 43.73 4511 N THR A 695 47.560 23.824 27.511 1.00 23.27 4512 CA THR A 695 46.427 24.609 27.898 1.00 24.00 4513 C THR A 695 45.076 23.936 27.789 1.00 21.80 4514 O THR A 695 44.094 24.597 28.158 1.00 23.18 4515 CB THR A 695 46.289 25.932 27.057 1.00 26.17 4516 OG1 THR A 695 45.835 25.571 25.738 1.00 30.11 4517 CG2 THR A 695 47.536 26.727 27.038 1.00 26.32 4518 N ALA A 696 44.970 22.725 27.246 1.00 17.97 4519 CA ALA A 696 43.659 22.141 27.079 1.00 19.04 4520 C ALA A 696 43.034 21.799 28.438 1.00 18.20 4521 O ALA A 696 43.750 21.502 29.404 1.00 17.08 4522 CB ALA A 696 43.747 20.900 26.195 1.00 18.12 4523 N GLN A 697 41.724 21.764 28.480 1.00 17.77 4524 CA GLN A 697 40.935 21.340 29.647 1.00 18.85 4525 C GLN A 697 40.214 20.039 29.320 1.00 19.35 4526 O GLN A 697 40.134 19.653 28.146 1.00 18.13 4527 CB GLN A 697 39.886 22.400 30.046 1.00 21.26 4528 CG GLN A 697 40.464 23.763 30.408 1.00 21.40 4529 CD GLN A 697 39.454 24.837 30.803 1.00 23.53 4530 OE1 GLN A 697 39.895 25.823 31.487 1.00 25.32 4531 NE2 GLN A 697 38.206 24.668 30.518 1.00 20.87 4532 N GLY A 698 39.716 19.300 30.312 1.00 18.21 4533 CA GLY A 698 38.991 18.051 30.069 1.00 16.88 4534 C GLY A 698 37.739 17.973 30.988 1.00 18.11 4535 O GLY A 698 37.289 19.027 31.463 1.00 18.21 4536 N PHE A 699 37.184 16.788 31.222 1.00 16.37 4537 CA PHE A 699 35.989 16.611 32.032 1.00 18.23 4538 C PHE A 699 36.113 17.182 33.445 1.00 18.02 4539 O PHE A 699 35.197 17.864 33.906 1.00 16.59 4540 CB PHE A 699 35.608 15.121 32.107 1.00 17.98 4541 CG PHE A 699 34.419 14.751 32.963 1.00 18.86 4542 CD1 PHE A 699 34.594 14.201 34.229 1.00 17.66 4543 CD2 PHE A 699 33.124 14.931 32.494 1.00 17.36 4544 CE1 PHE A 699 33.481 13.856 35.006 1.00 18.49 4645 CE2 PHE A 699 32.021 14.589 33.261 1.00 19.78 4546 CZ PHE A 699 32.189 14.044 34.525 1.00 19.39 4547 N ALA A 700 37.233 16.927 34.136 1.00 16.55 4548 CA ALA A 700 37.367 17.425 35.495 1.00 16.01 4549 C ALA A 700 37.613 18.922 35.560 1.00 17.98 4550 O ALA A 700 37.438 19.479 36.654 1.00 16.39 4551 CB ALA A 700 38.547 16.728 36.197 1.00 15.97 4552 N THR A 701 38.066 19.547 34.474 1.00 17.35 4553 CA THR A 701 38.531 20.920 34.525 1.00 18.55 4554 C THR A 701 37.744 21.889 33.629 1.00 19.85 4555 O THR A 701 38.226 23.004 33.458 1.00 20.14 4556 CB THR A 701 40.027 21.044 34.148 1.00 18.45 4557 OG1 THR A 701 40.289 20.404 32.895 1.00 18.96 4558 CG2 THR A 701 40.941 20.438 35.213 1.00 19.17 4559 N GLY A 702 36.558 21.526 33.166 1.00 21.54 4560 CA GLY A 702 35.692 22.478 32.466 1.00 23.96 4561 C GLY A 702 35.279 22.206 31.039 1.00 24.73 4562 O GLY A 702 34.407 22.929 30.527 1.00 23.67 4563 N ASP A 703 35.873 21.237 30.342 1.00 23.12 4564 CA ASP A 703 35.398 20.922 28.991 1.00 23.82 4565 C ASP A 703 34.070 20.187 29.093 1.00 23.19 4566 O ASP A 703 33.960 19.175 29.779 1.00 18.58 4567 CB ASP A 703 36.431 20.071 28.241 1.00 23.36 4568 CG ASP A 703 36.033 19.782 26.797 1.00 24.04 4569 OD1 ASP A 703 36.618 20.476 25.930 1.00 25.71 4570 OD2 ASP A 703 35.188 18.926 26.500 1.00 21.20 4571 N PRO A 704 33.059 20.609 28.324 1.00 24.11 4572 CA PRO A 704 31.731 20.018 28.400 1.00 23.04 4573 C PRO A 704 31.480 18.888 27.446 1.00 21.55 4574 O PRO A 704 30.401 18.265 27.492 1.00 21.23 4575 CB PRO A 704 30.809 21.220 28.065 1.00 24.82 4576 CG PRO A 704 31.633 21.977 27.058 1.00 25.35 4577 CD PRO A 704 33.080 21.823 27.468 1.00 24.45 4578 N ASN A 705 32.447 18.525 26.606 1.00 19.72 4579 CA ASN A 705 32.185 17.446 25.629 1.00 21.46 4580 C ASN A 705 32.802 16.090 25.927 1.00 23.27 4581 O ASN A 705 32.884 15.294 24.976 1.00 23.47 4582 CB ASN A 705 32.745 17.969 24.290 1.00 21.14 4583 CG ASN A 705 32.042 19.276 23.915 1.00 23.28 4584 OD1 ASN A 705 30.818 19.366 24.062 1.00 23.01 4585 ND2 ASN A 705 32.790 20.256 23.491 1.00 24.52 4586 N GLN A 706 33.030 15.688 27.187 1.00 21.97 4587 CA GLN A 706 33.650 14.375 27.459 1.00 21.06 4588 C GLN A 706 32.804 13.352 28.193 1.00 21.75 4589 O GLN A 706 33.297 12.317 28.660 1.00 20.03 4590 CB GLN A 706 34.918 14.683 28.310 1.00 20.55 4591 CG GLN A 706 35.854 15.729 27.750 1.00 19.45 4592 CD GLN A 706 36.345 15.354 26.363 1.00 23.83 4593 OE1 GLN A 706 36.610 14.155 26.140 1.00 24.34 4594 NE2 GLN A 706 36.463 16.280 25.413 1.00 22.80 4595 N VAL A 707 31.486 13.514 28.358 1.00 20.98 4596 CA VAL A 707 30.608 12.590 29.043 1.00 21.61 4597 C VAL A 707 30.703 11.153 28.513 1.00 23.14 4598 O VAL A 707 30.863 10.217 29.304 1.00 19.91 4599 CB VAL A 707 29.115 13.027 29.034 1.00 22.13 4600 CG1 VAL A 707 28.133 11.953 29.488 1.00 18.96 4601 CG2 VAL A 707 28.930 14.204 30.014 1.00 20.82 4602 N ASP A 708 30.635 10.964 27.180 1.00 23.14 4603 CA ASP A 708 30.701 9.604 26.647 1.00 22.35 4604 C ASP A 708 32.118 9.026 26.784 1.00 20.35 4605 O ASP A 708 32.175 7.813 26.913 1.00 18.36 4606 CB ASP A 708 30.249 9.493 25.190 1.00 24.86 4607 CG ASP A 708 28.777 9.849 25.041 1.00 28.73 4608 OD1 ASP A 708 27.911 9.562 25.888 1.00 29.20 4609 OD2 ASP A 708 28.457 10.460 24.000 1.00 32.49 4610 N VAL A 709 33.177 9.833 26.732 1.00 19.19 4611 CA VAL A 709 34.512 9.243 26.985 1.00 19.71 4612 C VAL A 709 34.616 8.739 28.443 1.00 18.90 4613 O VAL A 709 35.086 7.622 28.734 1.00 16.65 4614 CB VAL A 709 35.604 10.248 26.676 1.00 19.27 4615 CG1 VAL A 709 36.987 9.862 27.166 1.00 17.03 4616 CG2 VAL A 709 35.640 10.467 25.138 1.00 21.90 4617 N ILE A 710 34.165 9.578 29.376 1.00 17.70 4618 CA ILE A 710 34.132 9.165 30.786 1.00 17.02 4619 C ILE A 710 33.319 7.907 30.995 1.00 16.46 4620 O ILE A 710 33.789 6.942 31.644 1.00 15.43 4621 CB ILE A 710 33.641 10.356 31.640 1.00 16.39 4622 CG1 ILE A 710 34.615 11.533 31.483 1.00 19.18 4623 CG2 ILE A 710 33.543 9.944 33.100 1.00 16.50 4624 CD1 ILE A 710 36.090 11.238 31.712 1.00 15.64 4625 N LYS A 711 32.105 7.794 30.422 1.00 17.27 4626 CA LYS A 711 31.267 6.607 30.613 1.00 17.74 4627 C LYS A 711 31.972 5.347 30.102 1.00 17.56 4628 O LYS A 711 31.855 4.277 30.716 1.00 17.05 4629 CB LYS A 711 29.870 6.695 29.933 1.00 20.15 4630 CG LYS A 711 28.924 7.679 30.662 1.00 23.13 4631 CD LYS A 711 27.567 7.692 29.962 1.00 28.41 4632 CE LYS A 711 26.580 8.731 30.447 1.00 30.81 4633 NZ LYS A 711 25.271 8.572 29.682 1.00 34.74 4634 N ASN A 712 32.624 5.442 28.943 1.00 16.24 4635 CA ASN A 712 33.389 4.323 28.403 1.00 17.57 4636 C ASN A 712 34.537 3.949 29.358 1.00 16.07 4637 O ASN A 712 34.819 2.758 29.543 1.00 16.07 4638 CB ASN A 712 33.967 4.698 27.036 1.00 18.74 4639 CG ASN A 712 33.031 4.342 25.891 1.00 21.96 4640 OD1 ASN A 712 32.812 3.181 25.595 1.00 21.32 4641 ND2 ASN A 712 32.322 5.338 25.353 1.00 23.31 4642 N GLY A 713 35.160 4.910 30.029 1.00 15.84 4643 CA GLY A 713 36.196 4.574 31.026 1.00 15.68 4644 C GLY A 713 35.616 3.941 32.302 1.00 16.62 4645 O GLY A 713 36.235 3.026 32.905 1.00 15.22 4646 N VAL A 714 34.458 4.434 32.755 1.00 16.34 4647 CA VAL A 714 33.775 3.909 33.951 1.00 15.53 4648 C VAL A 714 33.490 2.430 33.793 1.00 15.76 4649 O VAL A 714 33.610 1.702 34.794 1.00 16.34 4650 CB VAL A 714 32.457 4.629 34.258 1.00 16.87 4651 CG1 VAL A 714 31.474 3.887 35.168 1.00 14.77 4652 CG2 VAL A 714 32.705 5.999 34.927 1.00 16.03 4653 N ILE A 715 33.060 1.928 32.632 1.00 16.13 4654 CA ILE A 715 32.769 0.468 32.556 1.00 15.59 4655 C ILE A 715 34.003 −0.389 32.207 1.00 16.37 4656 O ILE A 715 33.911 −1.557 31.784 1.00 14.09 4657 CB ILE A 715 31.619 0.207 31.554 1.00 15.72 4658 CG1 ILE A 715 31.997 0.689 30.136 1.00 15.41 4659 CG2 ILE A 715 30.315 0.959 31.967 1.00 15.73 4660 CD1 ILE A 715 30.904 0.480 29.056 1.00 17.76 4661 N GLY A 716 35.234 0.099 32.413 1.00 15.99 4662 CA GLY A 716 36.440 −0.726 32.202 1.00 14.94 4663 C GLY A 716 36.808 −0.841 30.730 1.00 15.94 4664 O GLY A 716 37.424 −1.833 30.314 1.00 16.36 4665 N SER A 717 36.394 0.105 29.882 1.00 13.02 4666 CA SER A 717 36.785 0.122 28.471 1.00 15.05 4667 C SER A 717 36.284 −1.033 27.650 1.00 15.07 4668 O SER A 717 36.690 −1.154 26.479 1.00 15.88 4669 CB SER A 717 38.379 0.196 28.479 1.00 12.88 4670 OG SER A 717 38.624 1.550 28.854 1.00 16.45 4671 N ILE A 718 35.335 −1.833 28.140 1.00 13.58 4672 CA ILE A 718 34.833 −3.017 27.485 1.00 16.06 4673 C ILE A 718 34.018 −2.762 26.216 1.00 18.30 4674 O ILE A 718 33.755 −3.690 25.423 1.00 17.12 4675 CB ILE A 718 33.972 −3.868 28.463 1.00 14.85 4676 CG1 ILE A 718 32.705 −3.102 28.902 1.00 14.22 4677 CG2 ILE A 718 34.803 −4.358 29.641 1.00 13.95 4678 CD1 ILE A 718 31.759 −3.997 29.708 1.00 14.94 4679 N GLN A 719 33.665 −1.511 25.966 1.00 20.52 4680 CA GLN A 719 33.070 −1.148 24.477 1.00 23.41 4681 C GLN A 719 34.019 −0.262 23.894 1.00 22.29 4682 O GLN A 719 33.605 0.413 22.972 1.00 21.69 4683 CB GLN A 719 31.726 −0.410 24.905 1.00 25.15 4684 CG GLN A 719 30.710 −1.398 25.487 1.00 29.75 4685 CD GLN A 719 30.193 −2.454 24.535 1.00 33.47 4686 OE1 GLN A 719 30.552 −2.581 23.370 1.00 34.39 4687 NE2 GLN A 719 29.279 −3.300 25.048 1.00 35.85 4688 N ASP A 720 35.274 −0.139 24.286 1.00 20.49 4689 CA ASP A 720 36.189 0.785 23.621 1.00 20.66 4690 C ASP A 720 37.361 −0.033 23.088 1.00 20.80 4691 O ASP A 720 37.521 −0.167 21.880 1.00 19.75 4692 CB ASP A 720 36.604 1.845 24.680 1.00 21.05 4693 CG ASP A 720 37.535 2.895 24.139 1.00 23.81 4694 OD1 ASP A 720 37.824 2.819 22.920 1.00 23.07 4695 OD2 ASP A 720 37.996 3.843 24.839 1.00 25.42 4696 N PHE A 721 38.162 −0.679 23.947 1.00 18.58 4697 CA PHE A 721 39.268 −1.508 23.422 1.00 18.29 4698 C PHE A 721 39.608 −2.722 24.262 1.00 19.42 4699 O PHE A 721 40.655 −3.321 23.961 1.00 18.82 4700 CB PHE A 721 40.557 −0.647 23.250 1.00 16.48 4701 CG PHE A 721 40.983 0.029 24.520 1.00 16.11 4702 CD1 PHE A 721 40.487 1.297 24.909 1.00 13.99 4703 CD2 PHE A 721 41.893 −0.659 25.356 1.00 17.14 4704 CE1 PHE A 721 40.966 1.833 26.081 1.00 14.66 4705 CE2 PHE A 721 42.282 −0.123 26.610 1.00 15.32 4706 CZ PHE A 721 41.772 1.078 26.959 1.00 14.52 4707 N THR A 722 38.806 −3.129 25.271 1.00 18.35 4708 CA THR A 722 39.234 −4.301 26.048 1.00 18.71 4709 C THR A 722 38.256 −5.465 25.964 1.00 20.07 4710 O THR A 722 37.131 −5.187 25.605 1.00 15.87 4711 CB THR A 722 39.370 −4.000 27.568 1.00 18.02 4712 OG1 THR A 722 38.074 −3.670 28.117 1.00 16.78 4713 CG2 THR A 722 40.327 −2.847 27.866 1.00 14.81 4714 N SER A 723 38.634 −6.684 26.382 1.00 20.49 4715 CA SER A 723 37.652 −7.760 26.508 1.00 20.59 4716 C SER A 723 37.348 −8.047 27.978 1.00 19.48 4717 O SER A 723 36.524 −8.903 28.269 1.00 18.62 4718 CB SER A 723 38.180 −9.078 25.911 1.00 24.40 4719 OG SER A 723 38.237 −8.849 24.496 1.00 30.69 4720 N ALA A 724 38.066 −7.402 28.893 1.00 18.21 4721 CA ALA A 724 37.899 −7.608 30.343 1.00 19.12 4722 C ALA A 724 38.520 −6.384 31.027 1.00 17.24 4723 O ALA A 724 39.416 −5.778 30.461 1.00 14.91 4724 CB ALA A 724 38.614 −8.866 30.799 1.00 18.06 4725 N PRO A 725 38.026 −5.999 32.198 1.00 16.70 4726 CA PRO A 725 38.492 −4.783 32.855 1.00 16.71 4727 C PRO A 725 39.952 −4.840 33.276 1.00 15.43 4728 O PRO A 725 40.587 −3.775 33.366 1.00 14.10 4729 CB PRO A 725 37.489 −4.587 33.975 1.00 16.43 4730 CG PRO A 725 37.007 −5.964 34.298 1.00 16.92 4731 CD PRO A 725 36.921 −6.642 32.931 1.00 16.63 4732 N SER A 726 40.558 −6.013 33.429 1.00 14.30 4733 CA SER A 726 41.982 −6.146 33.752 1.00 16.27 4734 C SER A 726 42.918 −5.644 32.664 1.00 17.17 4735 O SER A 726 44.114 −5.417 32.923 1.00 16.54 4736 CB SER A 726 42.327 −7.619 34.067 1.00 15.38 4737 OG SER A 726 42.016 −8.458 32.938 1.00 16.05 4738 N GLU A 727 42.424 −5.385 31.443 1.00 17.23 4739 CA GLU A 727 43.285 −4.934 30.337 1.00 15.75 4740 C GLU A 727 43.407 −3.427 30.227 1.00 16.68 4741 O GLU A 727 44.127 −2.965 29.335 1.00 16.11 4742 CB GLU A 727 42.733 −5.464 29.003 1.00 16.78 4743 CG GLU A 727 42.684 −7.007 28.978 1.00 15.52 4744 CD GLU A 727 41.939 −7.565 27.761 1.00 17.00 4745 OE1 GLU A 727 41.381 −6.829 26.934 1.00 15.44 4746 OE2 GLU A 727 41.889 −8.794 27.542 1.00 17.47 4747 N THR A 728 42.758 −2.643 31.103 1.00 13.84 4748 CA THR A 728 42.902 −1.194 30.999 1.00 15.17 4749 C THR A 728 43.571 −0.687 32.286 1.00 15.61 4750 O THR A 728 43.030 −0.930 33.380 1.00 15.14 4751 CB THR A 728 41.587 −0.424 30.739 1.00 14.97 4752 CG1 THR A 728 41.796 1.025 30.886 1.00 15.95 4753 CG2 THR A 728 40.515 −0.764 31.802 1.00 14.40 4754 N ILE A 729 44.667 0.062 32.166 1.00 14.75 4755 CA ILE A 729 45.295 0.716 33.325 1.00 14.43 4756 C ILE A 729 44.727 2.155 33.337 1.00 15.83 4757 O ILE A 729 45.145 2.937 32.453 1.00 17.36 4758 CB ILE A 729 46.818 0.776 33.179 1.00 15.12 4759 CG1 ILE A 729 47.417 −0.582 32.833 1.00 13.83 4760 CG2 ILE A 729 47.496 1.228 34.524 1.00 16.20 4761 CD1 ILE A 729 47.025 −1.766 33.724 1.00 11.75 4762 N ASN A 730 43.764 2.501 34.179 1.00 15.29 4763 CA ASN A 730 43.155 3.831 34.153 1.00 16.11 4764 C ASN A 730 44.036 4.865 34.850 1.00 15.71 4765 O ASN A 730 44.559 4.561 35.927 1.00 14.58 4766 CB ASN A 730 41.764 3.781 34.807 1.00 16.99 4767 CG ASN A 730 40.776 2.775 34.203 1.00 16.76 4768 OD1 ASN A 730 39.932 2.076 34.846 1.00 17.80 4769 ND2 ASN A 730 40.923 2.747 32.900 1.00 14.18 4770 N TYR A 731 44.303 6.022 34.261 1.00 14.78 4771 CA TYR A 731 45.135 7.013 34.912 1.00 16.43 4772 C TYR A 731 44.889 8.442 34.401 1.00 16.53 4773 O TYR A 731 44.321 8.554 33.309 1.00 16.09 4774 CB TYR A 731 46.641 6.738 34.752 1.00 16.77 4775 CG TYR A 731 47.189 6.951 33.358 1.00 17.72 4776 CD1 TYR A 731 48.208 7.865 33.101 1.00 18.91 4777 CD2 TYR A 731 46.723 6.190 32.306 1.00 16.97 4778 CE1 TYR A 731 48.689 8.074 31.810 1.00 20.50 4779 CE2 TYR A 731 47.152 6.393 31.015 1.00 19.21 4780 CZ TYR A 731 48.157 7.321 30.782 1.00 22.10 4781 OH TYR A 731 48.585 7.473 29.473 1.00 22.66 4782 N VAL A 732 45.463 9.396 35.150 1.00 14.45 4783 CA VAL A 732 45.429 10.782 34.652 1.00 15.94 4784 C VAL A 732 46.793 11.401 34.486 1.00 15.92 4785 O VAL A 732 46.949 12.340 33.663 1.00 16.20 4786 CB VAL A 732 44.507 11.667 35.541 1.00 16.99 4787 CG1 VAL A 732 44.997 11.697 36.988 1.00 13.37 4788 CG2 VAL A 732 44.444 13.123 35.006 1.00 17.23 4789 N THR A 733 47.822 11.034 35.242 1.00 15.69 4790 CA THR A 733 49.189 11.535 35.142 1.00 16.13 4791 C THR A 733 50.244 10.428 35.359 1.00 16.11 4792 O THR A 733 49.918 9.357 35.898 1.00 13.88 4793 CB THR A 733 49.597 12.657 36.115 1.00 17.42 4794 OG1 THR A 733 49.438 12.231 37.477 1.00 15.92 4795 CG2 THR A 733 48.827 13.958 35.888 1.00 14.57 4796 N SER A 734 51.504 10.693 34.974 1.00 16.76 4797 CA SER A 734 52.607 9.753 35.168 1.00 16.69 4798 C SER A 734 53.925 10.520 35.190 1.00 17.73 4799 O SER A 734 53.869 11.751 35.123 1.00 18.37 4800 CB SER A 734 52.699 8.630 34.116 1.00 16.19 4801 OG SER A 734 53.031 9.220 32.839 1.00 17.55 4802 N HIS A 735 55.095 9.901 35.332 1.00 16.87 4803 CA HIS A 735 56.355 10.627 35.335 1.00 18.13 4804 C HIS A 735 56.582 11.454 34.067 1.00 18.58 4805 O HIS A 735 57.307 12.484 34.165 1.00 20.77 4806 CB HIS A 735 57.585 9.714 35.570 1.00 16.15 4807 CG HIS A 735 57.897 8.867 34.358 1.00 16.14 4808 ND1 HIS A 735 57.309 7.621 34.171 1.00 13.70 4809 CD2 HIS A 735 58.707 9.141 33.286 1.00 14.91 4810 CE1 HIS A 735 57.772 7.135 33.010 1.00 16.16 4811 NE2 HIS A 735 58.586 8.039 32.480 1.00 16.01 4812 N ASP A 736 56.069 11.050 32.912 1.00 18.06 4813 CA ASP A 736 55.221 11.847 31.698 1.00 18.55 4814 C ASP A 736 55.296 13.073 31.785 1.00 19.59 4815 O ASP A 736 54.252 13.058 32.472 1.00 14.38 4816 CB ASP A 736 55.851 11.014 30.458 1.00 19.05 4817 CG ASP A 736 56.916 10.045 29.971 1.00 19.36 4818 OD1 ASP A 736 58.079 10.474 29.782 1.00 18.46 4819 OD2 ASP A 736 56.639 8.828 29.769 1.00 19.23 4820 N ASN A 737 55.648 14.149 31.055 1.00 19.40 4821 CA ASN A 737 54.827 15.353 31.031 1.00 19.79 4822 C ASN A 737 54.651 15.987 32.411 1.00 20.31 4823 O ASN A 737 55.545 15.914 33.270 1.00 18.64 4824 CB ASN A 737 53.499 15.028 30.295 1.00 20.11 4825 CG ASN A 737 53.794 14.336 28.972 1.00 23.21 4826 OD1 ASN A 737 53.500 13.160 28.760 1.00 23.28 4827 ND2 ASN A 737 54.473 14.985 28.022 1.00 23.64 4828 N MET A 738 53.530 16.651 32.711 1.00 19.26 4829 CA MET A 738 53.389 17.416 33.938 1.00 19.59 4830 C MET A 738 52.657 16.709 35.085 1.00 19.41 4831 O MET A 738 51.854 15.813 34.846 1.00 17.92 4832 CB MET A 738 52.619 18.711 33.619 1.00 20.83 4833 CG MET A 738 53.300 19.598 32.561 1.00 22.68 4834 SD MET A 738 52.260 21.070 32.188 1.00 25.13 4835 CE MET A 738 52.683 22.154 33.456 1.00 22.07 4836 N THR A 739 52.939 17.124 36.311 1.00 17.76 4837 CA THR A 739 52.155 16.614 37.447 1.00 18.00 4838 C THR A 739 50.770 17.275 37.332 1.00 18.02 4839 O THR A 739 50.609 18.312 36.672 1.00 18.06 4840 CB THR A 739 52.781 16.952 38.809 1.00 19.29 4841 OG1 THR A 739 52.642 18.358 39.103 1.00 17.62 4842 CG2 THR A 739 54.267 16.607 38.889 1.00 17.97 4843 N LEU A 740 49.739 16.694 37.916 1.00 16.11 4844 CA LEU A 740 48.403 17.232 37.843 1.00 17.22 4845 C LEU A 740 48.315 18.636 38.430 1.00 16.52 4846 O LEU A 740 47.642 19.447 37.769 1.00 17.44 4847 CB LEU A 740 47.300 16.323 38.417 1.00 15.94 4848 CG LEU A 740 45.862 16.743 38.020 1.00 16.72 4849 CD1 LEU A 740 45.757 16.769 36.484 1.00 16.81 4850 CD2 LEU A 740 44.836 15.720 38.527 1.00 14.02 4851 N TRP A 741 48.917 18.934 39.557 1.00 16.04 4852 CA TRP A 741 48.920 20.276 40.119 1.00 18.09 4853 C TRP A 741 49.452 21.316 39.117 1.00 20.12 4854 O TRP A 741 48.838 22.376 38.903 1.00 20.13 4855 CB TRP A 741 49.692 20.303 41.435 1.00 17.80 4856 CG TRP A 741 49.450 21.549 42.242 1.00 18.78 4857 CD1 TRP A 741 50.376 22.463 42.644 1.00 20.16 4858 CD2 TRP A 741 48.169 22.020 42.713 1.00 18.03 4859 NE1 TRP A 741 49.758 23.472 43.361 1.00 21.18 4860 CE2 TRP A 741 48.395 23.219 43.395 1.00 20.56 4861 CE3 TRP A 741 46.866 21.539 42.591 1.00 17.60 4862 CZ2 TRP A 741 47.368 23.961 44.000 1.00 20.50 4863 CZ3 TRP A 741 45.827 22.277 43.159 1.00 17.86 4864 CH2 TRP A 741 46.083 23.467 43.857 1.00 19.81 4865 N ASP A 742 50.582 21.019 38.485 1.00 19.17 4866 CA ASP A 742 51.203 21.880 37.484 1.00 19.35 4867 C ASP A 742 50.350 21.984 36.222 1.00 17.93 4868 O ASP A 742 50.146 23.081 35.724 1.00 16.62 4869 CB ASP A 742 52.592 21.376 37.082 1.00 18.32 4870 CG ASP A 742 53.612 21.544 38.183 1.00 18.67 4871 OD1 ASP A 742 53.279 21.975 39.300 1.00 19.97 4872 OD2 ASP A 742 54.794 21.167 38.023 1.00 18.27 4873 N LYS A 743 49.809 20.860 35.768 1.00 19.25 4874 CA LYS A 743 48.930 20.830 34.597 1.00 20.46 4875 C LYS A 743 47.680 21.685 34.812 1.00 20.53 4876 O LYS A 743 47.388 22.506 33.953 1.00 18.46 4877 CB LYS A 743 48.540 19.395 34.234 1.00 19.12 4878 CG LYS A 743 47.336 19.231 33.334 1.00 18.93 4879 CD LYS A 743 47.578 19.872 31.951 1.00 20.19 4880 CE LYS A 743 46.198 20.097 31.314 1.00 18.13 4881 NZ LYS A 743 46.312 20.465 29.867 1.00 16.42 4882 N ILE A 744 47.000 21.537 35.966 1.00 20.06 4883 CA ILE A 744 45.812 22.353 36.210 1.00 19.39 4884 C ILE A 744 46.150 23.835 36.365 1.00 20.80 4885 O ILE A 744 45.365 24.660 35.853 1.00 22.66 4886 CB ILE A 744 44.977 21.824 37.385 1.00 20.28 4887 CG1 ILE A 744 44.363 20.462 36.995 1.00 17.01 4888 CG2 ILE A 744 43.850 22.807 37.780 1.00 18.88 4889 CD1 ILE A 744 43.768 19.712 38.182 1.00 15.17 4890 N LEU A 745 47.292 24.254 36.899 1.00 19.68 4891 CA LEU A 745 47.690 25.652 36.898 1.00 23.49 4892 C LEU A 745 47.839 26.228 35.465 1.00 24.82 4893 O LEU A 745 47.471 27.398 35.201 1.00 23.41 4894 CB LEU A 745 49.072 25.836 37.539 1.00 24.77 4895 CG LEU A 745 49.509 27.212 37.976 1.00 28.42 4896 CD1 LEU A 745 48.531 27.865 38.985 1.00 28.65 4897 CD2 LEU A 745 50.857 27.244 38.702 1.00 29.02 4898 N ALA A 746 48.322 25.358 34.544 1.00 22.10 4899 CA ALA A 746 48.486 25.844 33.172 1.00 21.79 4900 C ALA A 746 47.184 25.938 32.398 1.00 21.61 4901 O ALA A 746 47.055 26.813 31.530 1.00 21.89 4902 CB ALA A 746 49.458 24.871 32.456 1.00 19.18 4903 N SER A 747 46.292 24.932 32.552 1.00 19.68 4904 CA SER A 747 45.040 24.968 31.851 1.00 19.92 4905 C SER A 747 44.016 25.873 32.565 1.00 20.35 4906 O SER A 747 43.053 26.199 31.881 1.00 19.89 4907 CB SER A 747 44.372 23.594 31.621 1.00 19.80 4908 OG SER A 747 44.018 22.968 32.866 1.00 22.16 4909 N ASN A 748 44.061 26.141 33.871 1.00 20.37 4910 CA ASN A 748 42.972 26.892 34.557 1.00 20.69 4911 C ASN A 748 43.616 27.982 35.418 1.00 21.19 4912 O ASN A 748 43.508 28.025 36.658 1.00 22.97 4913 CB ASN A 748 42.230 25.944 35.499 1.00 20.68 4914 CG ASN A 748 41.301 24.953 34.831 1.00 21.99 4915 OD1 ASN A 748 40.043 25.156 34.923 1.00 24.93 4916 ND2 ASN A 748 41.827 23.973 34.134 1.00 18.77 4917 N PRO A 749 44.412 28.851 34.819 1.00 22.66 4918 CA PRO A 749 45.192 29.825 35.564 1.00 24.77 4919 C PRO A 749 44.317 30.787 36.354 1.00 24.99 4920 O PRO A 749 44.780 31.208 37.413 1.00 28.37 4921 CB PRO A 749 46.076 30.507 34.506 1.00 23.57 4922 CG PRO A 749 45.240 30.423 33.269 1.00 25.06 4923 CD PRO A 749 44.574 29.067 33.359 1.00 22.65 4924 N SER A 750 43.100 31.111 35.973 1.00 27.45 4925 CA SER A 750 42.373 32.079 36.834 1.00 30.33 4926 C SER A 750 41.454 31.439 37.876 1.00 30.12 4927 O SER A 750 40.824 32.153 38.673 1.00 28.54 4928 CB SER A 750 41.708 33.101 35.932 1.00 30.51 4929 OG SER A 750 40.743 32.469 35.086 1.00 33.66 4930 N ASP A 751 41.410 30.106 37.977 1.00 27.22 4931 CA ASP A 751 40.591 29.469 39.011 1.00 25.49 4932 C ASP A 751 41.317 29.534 40.356 1.00 23.90 4933 O ASP A 751 42.551 29.566 40.384 1.00 21.81 4934 CB ASP A 751 40.251 28.035 38.640 1.00 25.71 4935 CG ASP A 751 39.119 27.964 37.643 1.00 27.68 4936 OD1 ASP A 751 38.017 28.510 37.899 1.00 29.06 4937 OD2 ASP A 751 39.317 27.350 36.581 1.00 27.19 4938 N THR A 752 40.546 29.584 41.463 1.00 21.83 4939 CA THR A 752 41.159 29.653 42.779 1.00 20.72 4940 C THR A 752 41.855 28.311 43.098 1.00 21.26 4941 O THR A 752 41.582 27.259 42.500 1.00 19.88 4942 CB THR A 752 40.151 29.916 43.915 1.00 20.18 4943 OG1 THR A 752 39.251 28.794 44.021 1.00 16.86 4944 CG2 THR A 752 39.235 31.142 43.708 1.00 18.66 4945 N GLU A 753 42.751 28.429 44.076 1.00 21.78 4946 CA GLU A 753 43.429 27.308 44.672 1.00 23.03 4947 C GLU A 753 42.430 26.254 45.153 1.00 21.75 4948 O GLU A 753 42.616 25.067 44.834 1.00 19.13 4949 CB GLU A 753 44.332 27.648 45.874 1.00 24.56 4950 CG GLU A 753 45.287 26.501 46.181 1.00 28.93 4951 CD GLU A 753 46.304 26.813 47.238 1.00 33.40 4952 OE1 GLU A 753 47.067 25.968 47.729 1.00 35.28 4953 OE2 GLU A 753 46.378 28.035 47.614 1.00 34.78 4954 N ALA A 754 41.408 26.715 45.929 1.00 19.55 4955 CA ALA A 754 40.439 25.748 46.423 1.00 18.95 4956 C ALA A 754 39.776 25.048 45.242 1.00 18.59 4957 O ALA A 754 39.434 23.831 45.331 1.00 16.89 4958 CB ALA A 754 39.358 26.388 47.347 1.00 17.73 4959 N ASP A 755 39.310 25.765 44.207 1.00 18.37 4960 CA ASP A 755 38.675 25.066 43.077 1.00 17.43 4961 C ASP A 755 39.646 24.137 42.339 1.00 18.14 4962 O ASP A 755 39.290 23.031 41.834 1.00 18.30 4963 CB ASP A 755 38.025 26.070 42.112 1.00 19.81 4964 CG ASP A 755 36.624 26.560 42.475 1.00 21.04 4965 OD1 ASP A 755 36.190 27.580 41.939 1.00 21.93 4966 OD2 ASP A 755 35.899 25.957 43.290 1.00 21.94 4967 N ARG A 756 40.914 24.503 42.188 1.00 18.10 4968 CA ARG A 756 41.891 23.655 41.478 1.00 16.46 4969 C ARG A 756 42.146 22.409 42.341 1.00 16.36 4970 O ARG A 756 42.201 21.306 41.780 1.00 14.27 4971 CB ARG A 756 43.168 24.439 41.108 1.00 17.08 4972 CG ARG A 756 42.898 25.555 40.071 1.00 20.15 4973 CD ARG A 756 44.176 26.286 39.593 1.00 21.05 4974 NE ARG A 756 44.608 27.330 40.496 1.00 22.58 4975 CZ ARG A 756 45.623 27.329 41.346 1.00 22.14 4976 NH1 ARG A 756 46.474 26.353 41.521 1.00 22.42 4977 NH2 ARG A 756 45.814 28.363 42.142 1.00 24.17 4978 N ILE A 757 42.144 22.500 43.688 1.00 15.45 4979 CA ILE A 757 42.170 21.297 44.521 1.00 15.56 4980 C ILE A 757 40.977 20.388 44.257 1.00 16.59 4981 O ILE A 757 41.151 19.162 43.993 1.00 16.56 4982 CB ILE A 757 42.316 21.636 46.034 1.00 17.09 4983 CG1 ILE A 757 43.755 22.055 46.341 1.00 15.23 4984 CG2 ILE A 757 41.894 20.412 46.892 1.00 16.32 4985 CD1 ILE A 757 44.008 22.725 47.668 1.00 16.53 4986 N LYS A 758 39.751 20.951 44.189 1.00 15.17 4987 CA LYS A 758 38.587 20.110 43.886 1.00 17.48 4988 C LYS A 758 38.686 19.381 42.557 1.00 16.06 4989 O LYS A 758 38.285 18.211 42.451 1.00 15.89 4990 CB LYS A 758 37.245 20.915 43.892 1.00 15.97 4991 CG LYS A 758 36.909 21.285 45.349 1.00 18.80 4992 CD LYS A 758 35.437 21.596 45.583 1.00 19.89 4993 CE LYS A 758 35.018 22.900 44.976 1.00 21.56 4994 NZ LYS A 758 33.521 22.969 44.892 1.00 23.65 4995 N MET A 759 39.199 20.079 41.536 1.00 15.74 4996 CA MET A 759 39.327 19.517 40.200 1.00 15.98 4997 C MET A 759 40.354 18.390 40.160 1.00 14.93 4998 O MET A 759 40.113 17.359 39.550 1.00 16.46 4999 CB MET A 759 39.733 20.623 39.208 1.00 17.07 5000 CG MET A 759 38.714 21.707 38.855 1.00 19.35 5001 SD MET A 759 39.471 23.010 37.839 1.00 19.26 5002 CE MET A 759 38.242 24.312 37.984 1.00 21.66 5003 N ASP A 760 41.459 18.508 40.908 1.00 16.22 5004 CA ASP A 760 42.480 17.450 41.007 1.00 16.26 5005 C ASP A 760 41.911 16.200 41.659 1.00 17.21 5006 O ASP A 760 42.042 15.049 41.214 1.00 17.75 5007 CB ASP A 760 43.645 18.034 41.819 1.00 17.31 5008 CG ASP A 760 44.913 17.214 41.946 1.00 17.03 5009 OD1 ASP A 760 44.793 15.983 42.065 1.00 15.47 5010 OD2 ASP A 760 46.047 17.756 41.909 1.00 14.89 5011 N GLU A 761 41.234 16.368 42.799 1.00 16.56 5012 CA GLU A 761 40.568 15.332 43.536 1.00 16.85 5013 C GLU A 761 39.469 14.695 42.670 1.00 16.63 5014 O GLU A 761 39.350 13.466 42.667 1.00 15.05 5015 CB GLU A 761 39.959 15.955 44.815 1.00 18.53 5016 CG GLU A 761 40.986 16.290 45.884 1.00 17.58 5017 CD GLU A 761 40.366 16.960 47.100 1.00 18.11 5018 OE1 GLU A 761 41.075 16.978 48.131 1.00 18.18 5019 OE2 GLU A 761 39.202 17.438 47.086 1.00 15.48 5020 N LEU A 762 38.681 15.476 41.908 1.00 14.32 5021 CA LEU A 762 37.725 14.847 40.991 1.00 15.45 5022 C LEU A 762 38.352 13.989 39.897 1.00 13.62 5023 O LEU A 762 37.806 12.922 39.595 1.00 13.44 5024 CB LEU A 762 36.841 15.905 40.308 1.00 16.49 5025 CG LEU A 762 35.804 15.442 39.294 1.00 20.45 5026 CD1 LEU A 762 34.763 14.500 39.907 1.00 18.27 5027 CD2 LEU A 762 35.059 16.623 38.651 1.00 20.38 5028 N ALA A 763 39.439 14.449 39.244 1.00 13.62 5029 CA ALA A 763 40.002 13.575 38.205 1.00 14.02 5030 C ALA A 763 40.440 12.248 38.843 1.00 13.98 5031 O ALA A 763 40.245 11.182 38.264 1.00 14.29 5032 CB ALA A 763 41.186 14.252 37.523 1.00 15.43 5033 N HIS A 764 41.107 12.268 39.991 1.00 13.75 5034 CA HIS A 764 41.529 11.018 40.633 1.00 14.85 5035 C HIS A 764 40.340 10.203 41.116 1.00 15.09 5036 O HIS A 764 40.318 8.959 41.071 1.00 14.64 5037 CB HIS A 764 42.523 11.373 41.764 1.00 16.48 5038 CG HIS A 764 43.881 11.820 41.290 1.00 16.16 5039 ND1 HIS A 764 44.861 10.897 40.931 1.00 17.78 5040 CD2 HIS A 764 44.425 13.045 41.106 1.00 14.29 5041 CE1 HIS A 764 45.980 11.539 40.576 1.00 13.10 5042 NE2 HIS A 764 45.734 12.822 40.663 1.00 18.06 5043 N ALA A 765 39.263 10.853 41.598 1.00 14.85 5044 CA ALA A 765 38.050 10.167 42.039 1.00 15.19 5045 C ALA A 765 37.481 9.281 40.923 1.00 15.79 5046 O ALA A 765 36.976 8.170 41.144 1.00 15.86 5047 CB ALA A 765 36.973 11.185 42.490 1.00 15.09 5048 N VAL A 766 37.426 9.768 39.691 1.00 15.11 5049 CA VAL A 766 37.011 8.984 38.524 1.00 14.49 5050 C VAL A 766 37.969 7.801 38.348 1.00 15.68 5051 O VAL A 766 37.484 6.669 38.206 1.00 15.59 5052 CB VAL A 766 36.967 9.813 37.215 1.00 14.83 5053 CG1 VAL A 766 36.639 8.953 35.976 1.00 13.21 5054 CG2 VAL A 766 35.898 10.921 37.371 1.00 13.49 5055 N VAL A 767 39.295 8.026 38.448 1.00 15.32 5056 CA VAL A 767 40.182 6.831 38.337 1.00 15.78 5057 C VAL A 767 39.874 5.778 39.405 1.00 16.72 5058 O VAL A 767 39.783 4.553 39.099 1.00 16.35 5059 CB VAL A 767 41.656 7.260 38.475 1.00 15.24 5060 CG1 VAL A 767 42.610 6.067 38.588 1.00 13.41 5061 CG2 VAL A 767 42.126 8.151 37.317 1.00 14.80 5062 N PHE A 768 39.717 6.221 40.658 1.00 16.27 5063 CA PHE A 768 39.471 5.305 41.772 1.00 16.07 5064 C PHE A 768 38.094 4.659 41.812 1.00 16.53 5065 O PHE A 768 37.996 3.555 42.413 1.00 15.80 5066 CB PHE A 768 39.838 5.868 43.137 1.00 15.94 5067 CG PHE A 768 41.238 6.460 43.307 1.00 16.54 5068 CD1 PHE A 768 41.402 7.676 43.923 1.00 15.00 5069 CD2 PHE A 768 42.374 5.808 42.882 1.00 17.09 5070 CE1 PHE A 768 42.654 8.258 44.120 1.00 16.04 5071 CE2 PHE A 768 43.640 6.366 43.042 1.00 17.04 5072 CZ PHE A 768 43.783 7.583 43.673 1.00 16.63 5073 N THR A 769 37.041 5.156 41.149 1.00 15.47 5074 CA THR A 769 35.736 4.475 41.230 1.00 14.36 5075 C THR A 769 35.328 3.823 39.920 1.00 15.61 5076 O THR A 769 34.198 3.269 39.801 1.00 15.87 5077 CB THR A 769 34.620 5.443 41.691 1.00 15.41 5078 OG1 THR A 769 34.713 6.617 40.902 1.00 14.96 5079 CG2 THR A 769 34.762 5.855 43.174 1.00 15.33 5080 N SER A 770 36.220 3.901 38.906 1.00 14.01 5081 CA SER A 770 35.921 3.261 37.631 1.00 14.16 5082 C SER A 770 36.302 1.788 37.682 1.00 14.69 5083 O SER A 770 37.326 1.408 38.247 1.00 13.64 5084 CB SER A 770 36.746 3.878 36.481 1.00 14.15 5085 OG SER A 770 36.278 5.140 36.080 1.00 11.78 5086 N GLN A 771 35.626 0.960 36.880 1.00 13.77 5087 CA GLN A 771 36.006 −0.422 36.664 1.00 13.99 5088 C GLN A 771 37.356 −0.464 35.925 1.00 15.46 5089 O GLN A 771 37.647 0.442 35.136 1.00 12.49 5090 CB GLN A 771 34.970 −1.223 35.849 1.00 13.53 5091 CG GLN A 771 33.544 −1.161 36.443 1.00 13.08 5092 CD GLN A 771 33.426 −1.789 37.822 1.00 14.69 5093 OE1 GLN A 771 32.830 −1.185 38.752 1.00 17.76 5094 NE2 GLN A 771 33.956 −2.976 38.040 1.00 10.21 5095 N GLY A 772 38.232 −1.456 36.210 1.00 15.16 5096 CA GLY A 772 39.559 −1.446 35.598 1.00 14.97 5097 C GLY A 772 40.698 −1.432 36.635 1.00 17.39 5098 O GLY A 772 40.444 −1.663 37.829 1.00 17.47 5099 N VAL A 773 41.944 −1.109 36.210 1.00 14.33 5100 CA VAL A 773 43.079 −1.067 37.150 1.00 14.45 5101 C VAL A 773 43.498 0.376 37.463 1.00 14.94 5102 O VAL A 773 44.084 0.998 36.611 1.00 16.35 5103 CB VAL A 773 44.310 −1.795 36.560 1.00 13.88 5104 CG1 VAL A 773 45.422 −1.889 37.632 1.00 14.66 5105 CG2 VAL A 773 44.005 −3.217 36.086 1.00 12.67 5106 N PRO A 774 43.257 0.966 38.599 1.00 13.58 5107 CA PRO A 774 43.649 2.341 38.928 1.00 15.84 5108 C PRO A 774 45.167 2.545 39.130 1.00 15.75 5109 O PRO A 774 45.813 1.748 39.817 1.00 15.14 5110 CB PRO A 774 42.834 2.611 40.199 1.00 14.18 5111 CG PRO A 774 42.710 1.231 40.899 1.00 14.41 5112 CD PRO A 774 42.527 0.274 39.729 1.00 13.83 5113 N PHE A 775 45.788 3.610 38.635 1.00 14.44 5114 CA PHE A 775 47.223 3.894 38.687 1.00 13.52 5115 C PHE A 775 47.368 5.379 39.009 1.00 15.10 5116 O PHE A 775 46.501 6.130 38.554 1.00 13.30 5117 CB PHE A 775 47.900 3.601 37.345 1.00 12.64 5118 CG PHE A 775 49.278 4.170 37.094 1.00 13.05 5119 CD1 PHE A 775 49.496 5.505 36.842 1.00 12.94 5120 CD2 PHE A 775 50.356 3.300 37.074 1.00 14.88 5121 CE1 PHE A 775 50.749 6.040 36.616 1.00 15.54 5122 CE2 PHE A 775 51.633 3.813 36.809 1.00 16.38 5123 CZ PHE A 775 51.828 5.157 36.592 1.00 15.45 5124 N MET A 776 48.332 5.763 39.836 1.00 14.40 5125 CA MET A 776 48.537 7.192 40.097 1.00 15.32 5126 C MET A 776 50.042 7.492 40.068 1.00 16.66 5127 O MET A 776 50.796 6.561 40.340 1.00 16.26 5128 CB MET A 776 47.999 7.42 41.453 1.00 14.34 5129 CG MET A 776 48.432 6.833 42.53 1.00 15.93 5130 SD MET A 776 47.677 7.342 44.233 1.00 13.48 5131 CE MET A 776 48.304 9.017 44.325 1.00 14.69 5132 N GLN A 777 50.420 8.732 39.804 1.00 16.06 5133 CA GLN A 777 51.838 9.108 39.931 1.00 15.06 5134 C GLN A 777 52.082 9.345 41.420 1.00 13.74 5135 O GLN A 777 51.281 10.097 41.996 1.00 12.00 5136 CB GLN A 777 52.175 10.388 39.136 1.00 15.88 5137 CG GLN A 777 53.660 10.809 39.318 1.00 14.21 5138 CD GLN A 777 54.081 12.028 38.491 1.00 16.72 5139 OE1 GLN A 777 55.294 12.354 38.396 1.00 15.28 5140 NE2 GLN A 777 53.132 12.777 37.931 1.00 13.34 5141 N GLY A 778 53.109 8.770 42.037 1.00 14.51 5142 CA GLY A 778 53.354 8.968 43.469 1.00 12.51 5143 C GLY A 778 53.552 10.434 43.782 1.00 15.81 5144 O GLY A 778 54.236 11.120 42.976 1.00 16.75 5145 N GLY A 779 52.939 10.912 44.890 1.00 14.32 5146 CA GLY A 779 53.108 12.345 45.197 1.00 14.20 5147 C GLY A 779 51.919 13.204 44.778 1.00 13.35 5148 O GLY A 779 51.774 14.341 45.263 1.00 13.40 5149 N GLU A 780 51.027 12.713 43.910 1.00 12.45 5150 CA GLU A 780 49.829 13.482 43.533 1.00 12.05 5151 C GLU A 780 48.913 13.718 44.746 1.00 14.09 5152 O GLU A 780 48.336 14.808 44.855 1.00 15.37 5153 CB GLU A 780 48.989 12.898 42.410 1.00 13.91 5154 CG GLU A 780 49.577 12.770 41.025 1.00 16.76 5155 CD GLU A 780 50.238 13.981 40.396 1.00 20.75 5156 OE1 GLU A 780 51.146 14.633 41.024 1.00 19.70 5157 OE2 GLU A 780 49.891 14.243 39.214 1.00 19.72 5158 N GLU A 781 48.866 12.843 45.725 1.00 14.52 5159 CA GLU A 781 48.154 12.941 46.974 1.00 15.90 5160 C GLU A 781 48.654 14.108 47.829 1.00 18.04 5161 O GLU A 781 47.923 14.505 48.739 1.00 16.36 5162 CB GLU A 781 48.261 11.644 47.797 1.00 15.13 5163 CG GLU A 781 49.627 11.402 48.399 1.00 16.08 5164 CD GLU A 781 50.695 10.808 47.504 1.00 16.18 5165 OE1 GLU A 781 51.749 10.429 48.068 1.00 16.29 5166 OE2 GLU A 781 50.534 10.719 46.283 1.00 13.64 5167 N MET A 782 49.842 14.681 47.552 1.00 18.10 5168 CA MET A 782 50.278 15.860 48.278 1.00 18.57 5169 C MET A 782 50.588 17.012 47.311 1.00 18.29 5170 O MET A 782 51.393 17.853 47.652 1.00 19.99 5171 CB MET A 782 51.460 15.657 49.216 1.00 19.24 5172 CG MET A 782 52.667 14.956 48.626 1.00 21.00 5173 SD MET A 782 53.939 14.548 49.843 1.00 19.47 5174 CE MET A 782 55.206 13.871 48.770 1.00 24.22 5175 N LEU A 783 49.947 17.109 46.165 1.00 17.38 5176 CA LEU A 783 50.155 18.163 45.193 1.00 18.72 5177 C LEU A 783 51.620 18.346 44.767 1.00 19.18 5178 O LEU A 783 52.145 19.459 44.641 1.00 18.25 5179 CB LEU A 783 49.475 19.451 45.699 1.00 17.56 5180 CG LEU A 783 48.014 19.300 46.199 1.00 17.76 5181 CD1 LEU A 783 47.488 20.670 46.671 1.00 17.88 5182 CD2 LEU A 783 47.044 18.790 45.147 1.00 17.03 5183 N ARG A 784 52.365 17.273 44.548 1.00 18.59 5184 CA ARG A 784 53.781 17.338 44.128 1.00 16.30 5185 C ARG A 784 53.899 18.310 42.947 1.00 16.06 5186 O ARG A 784 53.105 18.204 42.016 1.00 13.00 5187 CB ARG A 784 54.303 15.965 43.754 1.00 16.36 5188 CG ARG A 784 55.732 15.937 43.128 1.00 15.05 5189 CD ARG A 784 56.414 14.612 43.471 1.00 14.37 5190 NE ARG A 784 57.508 14.212 42.581 1.00 15.11 5191 CZ ARG A 784 57.463 13.745 41.344 1.00 15.39 5192 NH1 ARG A 784 56.328 13.510 40.649 1.00 14.22 5193 NH2 ARG A 784 58.620 13.430 40.733 1.00 14.18 5194 N THR A 785 54.889 19.199 42.961 1.00 16.44 5195 CA THR A 785 55.115 20.158 41.892 1.00 15.86 5196 C THR A 785 56.506 20.037 41.278 1.00 17.13 5197 O THR A 785 57.501 19.843 41.965 1.00 17.03 5198 CB THR A 785 54.867 21.626 42.325 1.00 16.69 5199 OG1 THR A 785 55.174 22.534 41.239 1.00 15.16 5200 CG2 THR A 785 55.649 22.074 43.552 1.00 17.25 5201 N LYS A 786 56.614 20.188 39.958 1.00 18.17 5202 CA LYS A 786 57.921 20.173 39.294 1.00 17.98 5203 C LYS A 786 58.229 21.610 38.838 1.00 19.45 5204 O LYS A 786 59.132 21.831 38.027 1.00 18.14 5205 CB LYS A 786 57.889 19.233 38.073 1.00 16.77 5206 CG LYS A 786 57.954 17.750 38.423 1.00 14.96 5207 CD LYS A 786 57.859 16.802 37.187 1.00 14.97 5208 CE LYS A 786 57.877 15.352 37.713 1.00 15.19 5209 NZ LYS A 786 57.719 14.341 36.641 1.00 16.24 5210 N GLY A 787 57.436 22.583 39.295 1.00 18.49 5211 CA GLY A 787 57.644 23.974 38.910 1.00 20.70 5212 C GLY A 787 57.258 24.206 37.454 1.00 22.88 5213 O GLY A 787 57.860 25.094 36.818 1.00 23.87 5214 N GLY A 788 56.399 23.347 36.861 1.00 21.35 5215 CA GLY A 788 56.109 23.489 35.452 1.00 21.36 5216 C GLY A 788 56.890 22.565 34.521 1.00 22.43 5217 O GLY A 788 56.521 22.424 33.344 1.00 22.35 5218 N ASN A 789 57.981 21.941 34.970 1.00 21.38 5219 CA ASN A 789 58.756 21.085 34.057 1.00 20.82 5220 C ASN A 789 57.880 20.009 33.441 1.00 22.07 5221 O ASN A 789 57.169 19.288 34.156 1.00 21.85 5222 CB ASN A 789 59.929 20.450 34.788 1.00 21.40 5223 CG ASN A 789 61.082 20.034 33.891 1.00 21.99 5224 OD1 ASN A 789 62.224 20.457 34.093 1.00 23.49 5225 ND2 ASN A 789 60.832 19.188 32.936 1.00 19.50 5226 N ASP A 790 57.941 19.850 32.117 1.00 21.23 5227 CA ASP A 790 57.167 18.811 31.470 1.00 22.38 5228 C ASP A 790 57.988 17.637 30.939 1.00 20.63 5229 O ASP A 790 57.393 16.915 30.142 1.00 19.94 5230 CB ASP A 790 56.287 19.374 30.343 1.00 26.38 5231 CG ASP A 790 57.068 19.930 29.177 1.00 30.47 5232 OD1 ASP A 790 56.515 20.793 28.455 1.00 33.68 5233 OD2 ASP A 790 58.222 19.566 28.904 1.00 31.34 5234 N ASN A 791 59.253 17.444 31.250 1.00 19.26 5235 CA ASN A 791 60.065 16.323 30.796 1.00 20.27 5236 C ASN A 791 61.345 16.285 31.637 1.00 21.29 5237 O ASN A 791 62.427 16.809 31.319 1.00 21.30 5238 CB ASN A 791 60.399 16.462 29.302 1.00 21.32 5239 CG ASN A 791 61.287 15.363 28.764 1.00 23.30 5240 OD1 ASN A 791 62.204 15.598 27.948 1.00 22.34 5241 ND2 ASN A 791 60.989 14.150 29.217 1.00 20.57 5242 N SER A 792 61.156 15.862 32.889 1.00 18.66 5243 CA SER A 792 62.048 15.872 34.014 1.00 18.76 5244 C SER A 792 63.218 14.927 34.077 1.00 17.02 5245 O SER A 792 63.795 14.823 35.171 1.00 15.69 5246 CB SER A 792 61.153 15.277 35.222 1.00 21.30 5247 OG SER A 792 60.809 16.404 35.929 1.00 26.39 5248 N TYR A 793 63.515 14.156 33.037 1.00 17.61 5249 CA TYR A 793 64.461 13.062 33.084 1.00 19.03 5250 C TYR A 793 65.842 13.343 33.677 1.00 19.80 5251 O TYR A 793 66.409 12.383 34.224 1.00 19.27 5252 CB TYR A 793 64.553 12.429 31.682 1.00 22.02 5253 CG TYR A 793 65.461 13.221 30.737 1.00 23.77 5254 CD1 TYR A 793 66.790 12.827 30.544 1.00 23.83 5255 CD2 TYR A 793 64.965 14.342 30.075 1.00 22.77 5256 CE1 TYR A 793 67.610 13.552 29.690 1.00 24.44 5257 CE2 TYR A 793 65.776 15.058 29.210 1.00 24.72 5258 CZ TYR A 793 67.098 14.657 29.040 1.00 24.81 5259 OH TYR A 793 67.896 15.388 28.191 1.00 26.96 5260 N ASN A 794 66.476 14.496 33.547 1.00 19.42 5261 CA ASN A 794 67.801 14.743 34.132 1.00 22.06 5262 C ASN A 794 67.762 16.039 34.931 1.00 22.30 5263 O ASN A 794 68.798 16.678 35.115 1.00 21.57 5264 CB ASN A 794 68.903 14.841 33.039 1.00 22.69 5265 CG ASN A 794 68.772 16.021 32.093 1.00 25.22 5266 OD1 ASN A 794 67.764 16.759 32.048 1.00 24.93 5267 ND2 ASN A 794 69.779 16.287 31.241 1.00 25.15 5268 N ALA A 795 66.562 16.450 35.392 1.00 22.67 5269 CA ALA A 795 66.383 17.734 36.035 1.00 21.37 5270 C ALA A 795 66.819 17.900 37.481 1.00 20.96 5271 O ALA A 795 66.796 19.075 37.914 1.00 20.75 5272 CB ALA A 795 64.896 18.177 35.919 1.00 19.65 5273 N GLY A 796 67.107 16.854 38.225 1.00 18.52 5274 CA GLY A 796 67.646 17.021 39.556 1.00 19.89 5275 C GLY A 796 66.566 16.955 40.632 1.00 19.49 5276 O GLY A 796 65.390 16.814 40.294 1.00 18.74 5277 N ASP A 797 66.989 17.117 41.871 1.00 18.66 5278 CA ASP A 797 66.128 16.903 43.044 1.00 20.03 5279 C ASP A 797 65.167 18.013 43.367 1.00 21.02 5280 O ASP A 797 63.994 17.803 43.701 1.00 20.32 5281 CB ASP A 797 67.067 16.594 44.244 1.00 19.80 5282 CG ASP A 797 68.007 15.440 44.019 1.00 19.46 5283 OD1 ASP A 797 69.230 15.521 44.326 1.00 21.24 5284 OD2 ASP A 797 67.633 14.351 43.526 1.00 20.79 5285 N SER A 798 65.560 19.280 43.210 1.00 21.85 5286 CA SER A 798 64.685 20.423 43.474 1.00 24.03 5287 C SER A 798 63.395 20.374 42.665 1.00 22.30 5288 O SER A 798 62.323 20.682 43.172 1.00 19.63 5289 CB SER A 798 65.451 21.739 43.216 1.00 27.04 5290 OG SER A 798 64.488 22.790 43.346 1.00 33.22 5291 N VAL A 799 63.473 19.840 41.450 1.00 19.85 5292 CA VAL A 799 62.354 19.588 40.579 1.00 19.39 5293 C VAL A 799 61.603 18.281 40.867 1.00 19.66 5294 O VAL A 799 60.379 18.346 40.925 1.00 18.31 5295 CB VAL A 799 62.837 19.448 39.110 1.00 19.45 5296 CG1 VAL A 799 61.707 19.105 38.147 1.00 17.83 5297 CG2 VAL A 799 63.547 20.738 38.692 1.00 20.77 5298 N ASN A 800 62.310 17.147 40.988 1.00 18.33 5299 CA ASN A 800 61.651 15.856 41.130 1.00 17.55 5300 C ASN A 800 61.376 15.299 42.514 1.00 16.34 5301 O ASN A 800 60.637 14.312 42.626 1.00 15.95 5302 CB ASN A 800 62.512 14.802 40.393 1.00 17.74 5303 CG ASN A 800 62.543 14.987 38.883 1.00 19.36 5304 OD1 ASN A 800 63.584 15.273 38.249 1.00 20.67 5305 ND2 ASN A 800 61.404 14.856 38.247 1.00 17.72 5306 N GLN A 801 61.969 15.783 43.590 1.00 14.69 5307 CA GLN A 801 61.866 15.102 44.861 1.00 18.63 5308 C GLN A 801 60.471 15.071 45.487 1.00 16.56 5309 O GLN A 801 59.644 15.874 45.101 1.00 15.25 5310 CB GLN A 801 62.806 15.707 45.932 1.00 17.66 5311 CG GLN A 801 62.342 17.090 46.382 1.00 19.69 5312 CD GLN A 801 63.483 17.927 46.966 1.00 21.59 5313 OE1 GLN A 801 64.500 17.414 47.435 1.00 22.85 5314 NE2 GLN A 801 63.304 19.240 47.068 1.00 21.07 5315 N PHE A 802 60.305 14.158 46.429 1.00 16.13 5316 CA PHE A 802 59.071 14.118 47.240 1.00 18.33 5317 C PHE A 802 59.323 15.192 48.327 1.00 18.45 5318 O PHE A 802 60.112 14.942 49.246 1.00 19.38 5319 CB PHE A 802 58.763 12.759 47.875 1.00 16.57 5320 CG PHE A 802 58.053 11.737 47.006 1.00 19.68 5321 CD1 PHE A 802 58.287 11.656 45.645 1.00 18.62 5322 CD2 PHE A 802 57.109 10.859 47.565 1.00 20.70 5323 CE1 PHE A 802 57.590 10.747 44.860 1.00 20.67 5324 CE2 PHE A 802 56.413 9.938 46.778 1.00 20.96 5325 CZ PHE A 802 56.693 9.865 45.429 1.00 19.43 5326 N ASP A 803 58.624 16.288 48.253 1.00 18.57 5327 CA ASP A 803 58.808 17.357 49.254 1.00 19.86 5328 C ASP A 803 57.793 17.081 50.357 1.00 20.28 5329 O ASP A 803 56.641 17.492 50.205 1.00 19.15 5330 CB ASP A 803 58.610 18.731 48.651 1.00 22.65 5331 CG ASP A 803 58.669 19.930 49.590 1.00 25.08 5332 OD1 ASP A 803 58.806 19.686 50.814 1.00 25.27 5333 OD2 ASP A 803 58.588 21.104 49.167 1.00 23.70 5334 N TRP A 804 58.233 16.380 51.405 1.00 18.05 5335 CA TRP A 804 57.319 15.921 52.445 1.00 19.41 5336 C TRP A 804 56.629 16.989 53.289 1.00 21.10 5337 O TRP A 804 55.653 16.669 53.993 1.00 19.44 5338 CB TRP A 804 57.946 14.789 53.243 1.00 18.06 5339 CG TRP A 804 58.290 13.537 52.497 1.00 19.31 5340 CD1 TRP A 804 59.477 13.263 51.863 1.00 18.88 5341 CD2 TRP A 804 57.474 12.380 52.297 1.00 19.81 5342 NE1 TRP A 804 59.448 12.034 51.283 1.00 18.40 5343 CE2 TRP A 804 58.216 11.461 51.531 1.00 18.59 5344 CE3 TRP A 804 56.163 12.061 52.677 1.00 18.95 5345 CZ2 TRP A 804 57.722 10.222 51.155 1.00 17.95 5346 CZ3 TRP A 804 55.674 10.809 52.304 1.00 18.76 5347 CH2 TRP A 804 56.437 9.922 51.551 1.00 17.47 5348 N SER A 805 57.047 18.260 63.210 1.00 21.38 5349 CA SER A 805 56.412 19.375 53.886 1.00 21.85 5350 C SER A 805 55.047 19.592 53.219 1.00 21.71 5351 O SER A 805 54.135 20.065 53.884 1.00 23.61 5352 CB SER A 805 57.197 20.695 53.829 1.00 19.87 5353 OG SER A 805 57.187 21.301 52.527 1.00 19.02 5354 N ARG A 806 54.822 19.172 51.974 1.00 19.88 5355 CA ARG A 806 53.512 19.335 51.351 1.00 22.24 5356 C ARG A 806 52.442 18.396 51.883 1.00 21.51 5357 O ARG A 806 51.254 18.722 51.750 1.00 19.94 5358 CB ARG A 806 53.636 19.156 49.822 1.00 24.11 5359 CG ARG A 806 54.034 20.543 49.260 1.00 26.24 5360 CD ARG A 806 54.401 20.399 47.801 1.00 24.25 5361 NE ARG A 806 53.327 20.788 46.893 1.00 21.27 5362 CZ ARG A 806 53.057 22.032 46.574 1.00 20.40 5363 NH1 ARG A 806 53.779 23.031 47.094 1.00 21.72 5364 NH2 ARG A 806 52.132 22.253 45.677 1.00 18.36 5365 N LYS A 807 52.841 17.251 52.437 1.00 20.38 5366 CA LYS A 807 51.865 16.365 53.068 1.00 20.37 5367 C LYS A 807 51.298 17.082 54.296 1.00 21.65 5368 O LYS A 807 50.107 17.019 54.552 1.00 21.63 5369 CB LYS A 807 52.501 15.007 53.414 1.00 17.10 5370 CG LYS A 807 51.504 14.093 54.081 1.00 18.69 5371 CD LYS A 807 52.030 12.677 54.344 1.00 16.56 5372 CE LYS A 807 50.960 11.883 55.134 1.00 15.71 5373 NE LYS A 807 51.497 10.512 55.378 1.00 14.68 5374 N ALA A 808 62.112 17.787 55.077 1.00 20.44 5375 CA ALA A 808 51.606 18.577 56.202 1.00 23.20 5376 C ALA A 808 50.732 19.752 55.729 1.00 22.93 5377 O ALA A 808 49.629 19.995 56.222 1.00 22.27 5378 CB ALA A 808 52.751 19.163 57.024 1.00 21.77 5379 N GLN A 809 51.188 20.477 54.706 1.00 23.92 5380 CA GLN A 809 50.492 21.617 54.146 1.00 23.89 5381 C GLN A 809 49.162 21.215 53.507 1.00 23.43 5382 O GLN A 809 48.168 21.944 53.608 1.00 20.37 5383 CB GLN A 809 51.356 22.355 53.095 1.00 25.14 5384 CG GLN A 809 50.627 23.521 52.421 1.00 26.75 5385 CD GLN A 809 51.547 24.361 51.551 1.00 29.36 5386 OE1 GLN A 809 52.735 24.031 51.422 1.00 28.08 5387 NE2 GLN A 809 51.050 25.449 60.941 1.00 30.28 5388 N PHE A 810 49.159 20.078 52.774 1.00 22.26 5389 CA PHE A 810 47.883 19.685 52.166 1.00 21.21 5390 C PHE A 810 47.375 18.387 52.769 1.00 21.19 5391 O PHE A 810 46.913 17.517 52.055 1.00 20.62 5392 CB PHE A 810 47.972 19.699 50.628 1.00 21.55 5393 CG PHE A 810 48.291 21.048 50.004 1.00 21.38 5394 CD1 PHE A 810 49.557 21.281 49.481 1.00 20.93 5395 CD2 PHE A 810 47.348 22.067 49.928 1.00 21.54 5396 CE1 PHE A 810 49.832 22.549 48.923 1.00 22.85 5397 CE2 PHE A 810 47.627 23.285 49.368 1.00 21.34 5398 CZ PHE A 810 48.881 23.543 48.856 1.00 22.67 5399 N LYS A 811 47.406 18.195 54.087 1.00 21.74 5400 CA LYS A 811 46.912 16.982 84.753 1.00 21.92 5401 C LYS A 811 45.455 16.673 54.422 1.00 21.36 5402 O LYS A 811 45.136 15.481 54.277 1.00 17.59 5403 CB LYS A 811 47.062 17.024 56.289 1.00 23.82 5404 CG LYS A 811 46.896 15.669 56.992 1.00 25.05 5405 CD LYS A 811 47.863 14.620 56.452 1.00 27.06 5406 CE LYS A 811 48.035 13.364 57.285 1.00 27.83 5407 NZ LYS A 811 46.792 12.947 57.977 1.00 30.70 5408 N ASP A 812 44.587 17.696 54.229 1.00 20.57 5409 CA ASP A 812 43.212 17.388 53.835 1.00 21.91 5410 C ASP A 812 43.149 16.742 52.456 1.00 20.65 5411 O ASP A 812 42.273 15.900 52.246 1.00 18.27 5412 CB ASP A 812 42.210 18.549 53.848 1.00 24.59 5413 CG ASP A 812 42.003 19.147 55.221 1.00 28.89 5414 OD1 ASP A 812 41.473 20.283 55.328 1.00 31.55 5415 OD2 ASP A 812 42.371 18.534 56.241 1.00 28.92 5416 N VAL A 813 44.036 17.111 51.539 1.00 18.77 5417 CA VAL A 813 44.040 16.444 50.227 1.00 18.35 5418 C VAL A 813 44.516 15.007 50.355 1.00 16.42 5419 O VAL A 813 43.987 14.074 49.741 1.00 16.64 5420 CB VAL A 813 44.922 17.275 49.264 1.00 19.35 5421 CG1 VAL A 813 44.998 16.618 47.885 1.00 16.35 5422 CG2 VAL A 813 44.486 18.742 49.166 1.00 19.07 5423 N PHE A 814 45.548 14.793 51.166 1.00 16.24 5424 CA PHE A 814 46.057 13.444 51.406 1.00 16.82 5425 C PHE A 814 44.943 12.573 51.982 1.00 17.46 5426 O PHE A 814 44.795 11.422 51.542 1.00 17.98 5427 CB PHE A 814 47.209 13.524 52.431 1.00 16.63 5428 CG PHE A 814 47.862 12.187 52.659 1.00 16.39 5429 CD1 PHE A 814 49.038 11.891 51.984 1.00 16.20 5430 CD2 PHE A 814 47.296 11.269 53.540 1.00 16.49 5431 CE1 PHE A 814 49.633 10.652 52.204 1.00 17.12 5432 CE2 PHE A 814 47.896 10.030 53.752 1.00 18.46 5433 CZ PHE A 814 49.062 9.746 53.077 1.00 18.20 5434 N ASP A 815 44.207 13.085 52.974 1.00 15.05 5435 CA ASP A 815 43.133 12.307 53.595 1.00 17.46 5436 C ASP A 815 42.017 11.960 52.607 1.00 16.89 5437 O ASP A 815 41.334 10.919 52.706 1.00 19.94 5438 CB ASP A 815 42.555 13.118 54.789 1.00 17.34 5439 CG ASP A 815 43.531 13.119 55.974 1.00 20.48 5440 OD1 ASP A 815 44.579 12.408 55.987 1.00 19.52 5441 OD2 ASP A 815 43.252 13.962 56.862 1.00 21.01 5442 N TYR A 816 41.683 12.885 51.710 1.00 16.33 5443 CA TYR A 816 40.663 12.564 50.678 1.00 16.00 5444 C TYR A 816 41.171 11.496 49.742 1.00 15.70 5445 O TYR A 816 40.397 10.580 49.417 1.00 16.79 5446 CB TYR A 816 40.309 13.837 49.869 1.00 16.36 5447 CG TYR A 816 39.217 13.680 48.824 1.00 15.25 5448 CD1 TYR A 816 39.444 13.129 47.564 1.00 15.93 5449 CD2 TYR A 816 37.918 14.077 49.117 1.00 15.92 5450 CE1 TYR A 816 38.400 12.970 46.633 1.00 15.05 5451 CE2 TYR A 816 36.886 13.958 48.209 1.00 16.61 5452 CZ TYR A 816 37.111 13.358 46.984 1.00 17.64 5453 OH TYR A 816 36.060 13.227 46.088 1.00 19.15 5454 N PHE A 817 42.434 11.487 49.320 1.00 12.51 5455 CA PHE A 817 42.962 10.474 48.436 1.00 13.42 5456 C PHE A 817 42.911 9.109 49.162 1.00 13.97 5457 O PHE A 817 42.435 8.133 48.606 1.00 13.72 5458 CB PHE A 817 44.389 10.643 47.942 1.00 13.63 5459 CG PHE A 817 44.578 11.514 46.713 1.00 12.99 5460 CD1 PHE A 817 45.189 10.988 45.577 1.00 14.35 5461 CD2 PHE A 817 44.228 12.837 46.732 1.00 14.28 5462 CE1 PHE A 817 45.442 11.773 44.444 1.00 14.16 5463 CE2 PHE A 817 44.474 13.644 45.615 1.00 15.25 5464 CZ PHE A 817 45.056 13.124 44.486 1.00 14.04 5465 N SER A 818 43.376 9.113 50.407 1.00 12.87 5466 CA SER A 818 43.354 7.917 51.238 1.00 15.48 5467 C SER A 818 41.955 7.389 51.512 1.00 14.72 5468 O SER A 818 41.744 6.162 51.485 1.00 16.73 5469 CB SER A 818 44.054 8.289 52.573 1.00 17.81 5470 OG SER A 818 43.841 7.176 53.431 1.00 22.91 5471 N SER A 819 40.963 8.251 51.745 1.00 15.04 5472 CA SER A 819 39.598 7.723 51.978 1.00 17.08 5473 C SER A 819 39.014 7.080 50.731 1.00 15.58 5474 O SER A 819 38.311 6.062 50.828 1.00 15.56 5475 CB SER A 819 38.630 8.852 52.401 1.00 18.73 5476 OG SER A 819 39.098 9.381 53.642 1.00 18.88 5477 N MET A 820 39.241 7.652 49.551 1.00 16.10 5478 CA MET A 820 38.739 7.072 48.304 1.00 18.56 5479 C MET A 820 39.374 5.710 48.019 1.00 18.57 5480 O MET A 820 38.727 4.747 47.598 1.00 16.01 5481 CB MET A 820 39.001 8.018 47.123 1.00 20.82 5482 CG MET A 820 38.153 7.749 45.900 1.00 23.16 5483 SD MET A 820 36.405 8.041 45.961 1.00 22.93 5484 CE MET A 820 36.118 9.783 45.834 1.00 23.13 5485 N ILE A 821 40.688 5.642 48.244 1.00 17.40 5486 CA ILE A 821 41.451 4.412 48.042 1.00 16.52 5487 C ILE A 821 41.001 3.334 49.035 1.00 16.03 5488 O ILE A 821 40.730 2.223 48.588 1.00 14.41 5489 CB ILE A 821 42.975 4.656 48.056 1.00 15.70 5490 CG1 ILE A 821 43.474 5.516 46.885 1.00 13.40 5491 CG2 ILE A 821 43.644 3.255 48.054 1.00 15.43 5492 CD1 ILE A 821 44.782 6.262 47.154 1.00 11.03 5493 N HIS A 822 40.778 3.678 50.314 1.00 14.76 5494 CA HIS A 822 40.300 2.633 51.237 1.00 16.65 5495 C HIS A 822 38.874 2.147 50.890 1.00 18.07 5496 O HIS A 822 38.504 0.977 51.044 1.00 16.15 5497 CB HIS A 822 40.389 3.195 52.667 1.00 18.28 5498 CG HIS A 822 41.797 3.237 53.209 1.00 18.71 5499 ND1 HIS A 822 42.240 2.252 54.074 1.00 22.35 5500 CD2 HIS A 822 42.825 4.101 53.055 1.00 17.41 5501 CE1 HIS A 822 43.525 2.504 54.403 1.00 19.56 5502 NE2 HIS A 822 43.884 3.652 53.816 1.00 20.90 5503 N LEU A 823 38.009 3.101 50.498 1.00 14.46 5504 CA LEU A 823 36.670 2.802 50.021 1.00 15.73 5505 C LEU A 823 36.756 1.864 48.847 1.00 15.38 5506 O LEU A 823 36.209 0.707 49.030 1.00 15.40 5507 CB LEU A 823 35.882 4.028 49.576 1.00 19.45 5508 CG LEU A 823 34.486 3.700 49.019 1.00 21.92 5509 CD1 LEU A 823 33.474 3.712 50.151 1.00 25.56 5510 CD2 LEU A 823 34.106 4.685 47.925 1.00 25.24 5511 N ARG A 824 37.475 2.025 47.744 1.00 14.25 5512 CA ARG A 824 37.617 0.995 46.740 1.00 13.61 5513 C ARG A 824 38.197 −0.307 47.284 1.00 14.10 5514 O ARG A 824 37.659 −1.363 46.894 1.00 15.81 5515 CB ARG A 824 38.584 1.423 45.592 1.00 13.50 5516 CG ARG A 824 38.612 0.463 44.411 1.00 12.90 5517 CD ARG A 824 39.803 0.839 43.450 1.00 14.06 5518 NE ARG A 824 39.853 −0.095 42.310 1.00 12.64 5519 CZ ARG A 824 39.049 −0.024 41.238 1.00 14.31 5520 NH1 ARG A 824 38.127 0.944 41.136 1.00 13.55 5521 NH2 ARG A 824 39.174 −0.928 40.254 1.00 14.66 5522 N ASN A 825 39.145 −0.268 48.232 1.00 14.31 5523 CA ASN A 825 39.689 −1.523 48.760 1.00 16.54 5524 C ASN A 825 38.644 −2.390 49.496 1.00 15.73 5525 O ASN A 825 38.693 −3.608 49.448 1.00 12.95 5526 CB ASN A 825 40.877 −1.380 49.720 1.00 14.70 5527 CG ASN A 825 42.129 −0.771 49.136 1.00 17.12 5528 OD1 ASN A 825 42.988 −0.200 49.853 1.00 19.07 5529 ND2 ASN A 825 42.310 −0.737 47.823 1.00 13.10 5530 N GLN A 826 37.741 −1.663 50.181 1.00 18.02 5531 CA GLN A 826 36.695 −2.358 50.934 1.00 20.90 5532 C GLN A 826 35.477 −2.876 50.182 1.00 20.36 5533 O GLN A 826 34.651 −3.630 50.742 1.00 19.69 5534 CB GLN A 826 36.132 −1.381 51.993 1.00 26.32 5535 CG GLN A 826 36.580 −1.691 53.397 1.00 35.56 5536 CD GLN A 826 36.182 −3.094 53.844 1.00 39.06 5537 OE1 GLN A 826 35.589 −3.891 53.119 1.00 42.26 5538 NE2 GLN A 826 36.412 −3.345 55.128 1.00 41.91 5539 N HIS A 827 35.234 −2.404 48.976 1.00 16.91 5540 CA HIS A 827 34.036 −2.689 48.202 1.00 16.78 5541 C HIS A 827 34.350 −3.273 46.840 1.00 15.74 5542 O HIS A 827 34.555 −2.536 45.872 1.00 13.89 5543 CB HIS A 827 33.257 −1.326 48.096 1.00 15.20 5544 CG HIS A 827 32.617 −0.988 49.413 1.00 16.26 5545 ND1 HIS A 827 33.202 −0.101 50.300 1.00 20.12 5546 CD2 HIS A 827 31.489 −1.420 50.032 1.00 14.76 5547 CE1 HIS A 827 32.440 0.011 51.389 1.00 16.71 5548 NE2 HIS A 827 31.427 −0.829 51.254 1.00 19.08 5549 N PRO A 828 34.325 −4.608 46.724 1.00 15.11 5550 CA PRO A 828 34.560 −5.321 45.497 1.00 14.14 5551 C PRO A 828 33.561 −5.010 44.393 1.00 15.45 5552 O PRO A 828 33.881 −5.329 43.255 1.00 15.72 5553 CB PRO A 828 34.468 −6.783 45.898 1.00 16.09 5554 CG PRO A 828 33.621 −6.815 47.163 1.00 14.98 5555 CD PRO A 828 34.044 −5.548 47.851 1.00 14.73 5556 N ALA A 829 32.423 −4.314 44.452 1.00 14.28 5557 CA ALA A 829 31.572 −3.851 43.558 1.00 14.18 5556 C ALA A 829 32.312 −2.961 42.554 1.00 15.27 5559 O ALA A 829 31.927 −2.910 41.374 1.00 14.49 5560 CB ALA A 829 30.396 −3.007 44.068 1.00 10.50 5561 N PHE A 830 33.342 −2.252 43.022 1.00 15.95 5562 CA PHE A 830 34.152 −1.385 42.170 1.00 16.15 5563 C PHE A 830 35.195 −2.117 41.342 1.00 16.91 5564 O PHE A 830 35.922 −1.562 40.474 1.00 15.96 5565 CB PHE A 830 34.922 −0.393 43.124 1.00 17.49 5566 CG PHE A 830 33.982 0.683 43.674 1.00 18.77 5567 CD1 PHE A 830 33.498 1.663 42.823 1.00 17.67 5568 CD2 PHE A 830 33.671 0.733 45.029 1.00 19.33 5569 CE1 PHE A 830 32.667 2.668 43.352 1.00 18.46 5570 CE2 PHE A 830 32.777 1.688 45.534 1.00 18.20 5571 CZ PHE A 830 32.304 2.663 44.685 1.00 18.78 5572 N ARG A 831 35.349 −3.406 41.627 1.00 15.44 5573 CA ARG A 831 36.378 −4.252 41.039 1.00 16.14 5574 C ARG A 831 35.894 −5.556 40.438 1.00 16.54 5575 O ARG A 831 36.425 −6.657 40.688 1.00 16.91 5576 CB ARG A 831 37.362 −4.574 42.188 1.00 16.96 5577 CG ARG A 831 38.080 −3.419 42.858 1.00 16.46 5578 CD ARG A 831 38.971 −3.779 44.005 1.00 17.94 5579 NE ARG A 831 38.365 −3.942 45.328 1.00 17.80 5580 CZ ARG A 831 38.198 −5.082 45.971 1.00 18.41 5581 NH1 ARG A 831 38.542 −6.244 45.421 1.00 18.63 5582 NH2 ARG A 831 37.617 −5.115 47.169 1.00 18.47 5583 N MET A 832 34.819 −5.468 39.649 1.00 16.98 5584 CA MET A 832 34.280 −6.623 38.923 1.00 16.56 5585 C MET A 832 35.367 −7.141 37.961 1.00 17.92 5586 O MET A 832 36.184 −6.323 37.488 1.00 17.69 5587 CB MET A 832 33.002 −6.169 38.210 1.00 16.53 5588 CG MET A 832 31.834 −5.953 39.241 1.00 15.93 5589 SD MET A 832 38.273 −5.688 38.352 1.00 14.50 5590 CE MET A 832 38.215 −3.878 38.401 1.00 13.68 5591 N THR A 833 35.416 −8.448 37.714 1.00 16.30 5592 CA THR A 833 36.465 −8.992 36.872 1.00 17.66 5593 C THR A 833 36.119 −9.364 35.440 1.00 19.22 5594 O THR A 833 37.057 −9.531 34.621 1.00 17.30 5595 CB THR A 833 37.064 −10.227 37.580 1.00 17.12 5596 OG1 THR A 833 36.053 −11.222 37.737 1.00 18.20 5597 CG2 THR A 833 37.634 −9.883 38.959 1.00 16.91 5598 N THR A 834 34.820 −9.464 35.089 1.00 17.86 5599 CA THR A 834 34.456 −9.796 33.723 1.00 19.46 5600 C THR A 834 33.566 −8.753 33.065 1.00 18.40 5601 O THR A 834 32.831 −8.851 33.768 1.00 18.40 5602 CB THR A 834 33.710 −11.144 33.592 1.00 19.44 5603 OG1 THR A 834 32.393 −10.968 34.125 1.00 20.68 5604 CG2 THR A 834 34.421 −12.276 34.309 1.00 19.43 5605 N ALA A 835 33.566 −8.699 31.732 1.00 19.48 5606 CA ALA A 835 32.648 −7.883 31.033 1.00 20.00 5607 C ALA A 835 31.193 −8.165 31.312 1.00 20.77 5608 O ALA A 835 38.385 −7.248 31.410 1.00 22.50 5609 CB ALA A 835 32.842 −7.825 29.508 1.00 18.74 5610 N ASP A 836 38.790 −9.421 31.421 1.00 22.07 5611 CA ASP A 836 29.447 −9.864 31.696 1.00 23.30 5612 C ASP A 836 28.969 −9.388 33.066 1.00 21.99 5613 O ASP A 836 27.808 −9.041 33.223 1.00 22.47 5614 CB ASP A 836 29.282 −11.410 31.664 1.00 25.61 5615 CG ASP A 836 29.189 −11.927 30.230 1.00 27.82 5616 OD1 ASP A 836 29.351 −13.158 30.024 1.00 30.02 5617 OD2 ASP A 836 29.058 −11.147 29.276 1.00 26.35 5618 N GLN A 837 29.844 −9.318 34.063 1.00 21.84 5619 CA GLN A 837 29.453 −8.854 35.377 1.00 20.02 5620 C GLN A 837 29.051 −7.386 35.296 1.00 18.66 5621 O GLN A 837 28.053 −7.047 35.906 1.00 17.00 5622 CB GLN A 837 30.603 −8.904 36.400 1.00 21.90 5623 CG GLN A 837 30.712 −10.131 37.263 1.00 22.49 5624 CD GLN A 837 31.790 −9.982 38.343 1.00 21.99 5625 OE1 GLN A 837 32.918 −9.616 38.024 1.00 20.17 5626 NE2 GLN A 837 31.367 −10.297 39.564 1.00 20.64 5627 N ILE A 838 29.898 −6.608 34.623 1.00 16.54 5628 CA ILE A 838 29.667 −5.167 34.499 1.00 18.19 5629 C ILE A 838 28.370 −4.877 33.740 1.00 20.92 5630 O ILE A 838 27.578 −3.998 34.152 1.00 18.47 5631 CB ILE A 838 30.895 −4.516 33.835 1.00 19.11 5632 CG1 ILE A 838 32.141 −4.578 34.778 1.00 16.48 5633 CG2 ILE A 838 30.618 −3.062 33.428 1.00 18.17 5634 CD1 ILE A 838 33.422 −4.259 33.992 1.00 16.81 5635 N LYS A 839 28.126 −5.604 32.642 1.00 28.48 5636 CA LYS A 839 26.868 −5.425 31.895 1.00 24.85 5637 C LYS A 839 25.681 −5.781 32.770 1.00 25.13 5638 O LYS A 839 24.646 −5.116 32.756 1.00 26.96 5639 CB LYS A 839 26.836 −6.328 30.636 1.00 24.14 5640 CG LYS A 839 27.894 −5.833 29.641 1.00 26.39 5641 CD LYS A 839 27.580 −6.351 28.235 1.00 30.49 5642 CE LYS A 839 28.219 −7.705 28.025 1.00 32.93 5643 NZ LYS A 839 28.865 −7.658 26.661 1.00 35.80 5644 N GLN A 840 25.788 −6.819 33.588 1.00 25.00 5645 CA GLN A 840 24.684 −7.184 34.471 1.00 26.52 5646 C GLN A 840 24.438 −6.235 35.642 1.00 24.27 5647 O GLN A 840 23.285 −6.041 36.067 1.00 21.92 5648 CB GLN A 840 25.070 −8.548 35.028 1.00 31.74 5649 CG GLN A 840 23.972 −9.403 35.610 1.00 39.43 5650 CD GLN A 840 24.253 −10.889 35.404 1.00 43.34 5651 OE1 GLN A 840 23.875 −11.733 36.232 1.00 45.14 5652 NE2 GLN A 840 24.920 −11.257 34.306 1.00 44.87 5653 N ASN A 841 25.494 −5.678 36.234 1.00 17.87 5654 CA ASN A 841 25.352 −4.940 37.483 1.00 19.33 5655 C ASN A 841 25.456 −3.442 37.474 1.00 17.58 5656 O ASN A 841 25.171 −2.831 38.520 1.00 17.51 5657 CB ASN A 841 26.468 −5.479 38.436 1.00 20.01 5658 CG ASN A 841 26.318 −6.928 38.823 1.00 21.30 5659 OD1 ASN A 841 27.336 −7.581 39.153 1.00 24.17 5660 ND2 ASN A 841 25.136 −7.506 38.867 1.00 17.31 5661 N LEU A 842 25.969 −2.825 36.425 1.00 17.66 5662 CA LEU A 842 26.184 −1.376 36.377 1.00 17.63 5663 C LEU A 842 25.163 −0.724 35.461 1.00 18.99 5664 O LEU A 842 25.011 −1.186 34.306 1.00 17.85 5665 CB LEU A 842 27.657 −1.086 35.967 1.00 16.31 5666 CG LEU A 842 28.122 0.412 36.099 1.00 16.16 5667 CD1 LEU A 842 29.646 0.464 36.201 1.00 15.40 5668 CD2 LEU A 842 27.670 1.171 34.847 1.00 16.66 5669 N THR A 843 24.433 0.335 35.896 1.00 18.55 5670 CA THR A 843 23.509 0.996 34.955 1.00 19.55 5671 C THR A 843 23.799 2.485 35.083 1.00 18.14 5672 O THR A 843 23.954 2.940 36.217 1.00 18.37 5673 CB THR A 843 21.997 0.715 35.324 1.00 21.75 5674 OG1 THR A 843 21.984 0.728 36.780 1.00 27.30 5675 CG2 THR A 843 21.591 −0.733 35.145 1.00 20.25 5676 N PHE A 844 23.800 3.289 34.050 1.00 17.73 5677 CA PHE A 844 23.831 4.740 34.087 1.00 17.70 5678 C PHE A 844 22.432 5.276 34.395 1.00 19.50 5679 O PHE A 844 21.404 4.713 33.999 1.00 17.81 5680 CB PHE A 844 24.393 5.290 32.769 1.00 19.16 5681 CG PHE A 844 25.890 4.994 32.659 1.00 18.93 5682 CD1 PHE A 844 26.336 3.998 31.778 1.00 19.58 5683 CD2 PHE A 844 26.805 5.688 33.423 1.00 16.70 5684 CE1 PHE A 844 27.691 3.718 31.666 1.00 17.53 5685 CE2 PHE A 844 28.161 5.407 33.322 1.00 16.61 5686 CZ PHE A 844 28.604 4.408 32.474 1.00 16.03 5687 N LEU A 845 22.317 6.283 35.262 1.00 20.29 5688 CA LEU A 845 21.038 6.840 35.660 1.00 21.27 5689 C LEU A 845 20.919 8.200 34.954 1.00 23.53 5690 O LEU A 845 21.935 8.833 34.636 1.00 23.88 5691 CB LEU A 845 20.935 7.051 37.170 1.00 21.66 5692 CG LEU A 845 21.162 5.826 38.092 1.00 23.12 5693 CD1 LEU A 845 21.274 6.272 39.546 1.00 22.17 5694 CD2 LEU A 845 20.052 4.791 37.920 1.00 23.11 5695 N GLU A 846 19.690 8.626 34.698 1.00 21.38 5696 CA GLU A 846 19.490 9.929 34.070 1.00 24.30 5697 C GLU A 846 19.991 11.035 34.975 1.00 21.71 5698 O GLU A 846 19.653 11.010 36.172 1.00 20.11 5699 CB GLU A 846 17.975 10.166 33.842 1.00 28.61 5700 CG GLU A 846 17.724 11.373 32.965 1.00 34.76 5701 CD GLU A 846 17.726 12.749 33.588 1.00 39.53 5702 OE1 GLU A 846 18.229 13.687 32.884 1.00 41.56 5703 OE2 GLU A 846 17.272 13.005 34.732 1.00 40.66 5704 N SER A 847 20.680 12.026 34.430 1.00 19.82 5705 CA SER A 847 21.208 13.081 35.319 1.00 18.64 5706 C SER A 847 21.368 14.319 34.462 1.00 19.77 5707 O SER A 847 21.263 14.210 33.233 1.00 18.46 5708 CB SER A 847 22.527 12.667 36.002 1.00 17.95 5709 OG SER A 847 23.592 12.595 35.047 1.00 19.81 5710 N PRO A 848 21.622 15.466 35.068 1.00 20.84 5711 CA PRO A 848 21.738 16.711 34.326 1.00 21.84 5712 C PRO A 848 22.900 16.792 33.349 1.00 24.33 5713 O PRO A 848 23.896 16.064 33.439 1.00 22.58 5714 CB PRO A 848 21.911 17.756 35.428 1.00 21.32 5715 CG PRO A 848 21.153 17.200 36.614 1.00 21.13 5716 CD PRO A 848 21.503 15.705 36.538 1.00 20.99 5717 N THR A 849 22.785 17.738 32.406 1.00 24.17 5718 CA THR A 849 23.849 17.972 31.424 1.00 24.95 5719 C THR A 849 25.242 18.088 32.050 1.00 22.16 5720 O THR A 849 25.493 18.737 33.071 1.00 21.14 5721 CB THR A 849 23.540 19.287 30.661 1.00 24.81 5722 OG1 THR A 849 22.271 19.114 30.029 1.00 25.94 5723 CG2 THR A 849 24.626 19.557 29.609 1.00 25.93 5724 N ASN A 850 26.201 17.420 31.423 1.00 20.59 5725 CA ASN A 850 27.600 17.432 31.834 1.00 20.77 5726 C ASN A 850 27.795 16.847 33.239 1.00 19.84 5727 O ASN A 850 28.665 17.266 34.020 1.00 18.02 5728 CB ASN A 850 28.286 18.778 31.664 1.00 20.31 5729 CG ASN A 850 29.817 18.702 31.663 1.00 21.52 5730 OD1 ASN A 850 30.384 17.768 31.100 1.00 19.79 5731 ND2 ASN A 850 30.504 19.668 32.261 1.00 18.52 5732 N THR A 851 27.040 15.769 33.508 1.00 18.54 5733 CA THR A 851 27.234 14.985 34.728 1.00 19.54 5734 C THR A 851 27.138 13.496 34.402 1.00 19.84 5735 O THR A 851 26.541 13.150 33.375 1.00 18.01 5736 CB THR A 851 26.235 15.237 35.873 1.00 18.24 5737 OG1 THR A 851 24.907 14.853 35.442 1.00 20.28 5738 CG2 THR A 851 26.248 16.692 36.320 1.00 18.83 5739 N VAL A 852 27.723 12.627 35.230 1.00 18.35 5740 CA VAL A 852 27.673 11.190 34.978 1.00 18.50 5741 C VAL A 852 27.277 10.516 36.296 1.00 19.16 5742 O VAL A 852 28.012 10.724 37.265 1.00 16.89 5743 CB VAL A 852 29.064 10.638 34.571 1.00 20.21 5744 CG1 VAL A 852 29.058 9.112 34.604 1.00 18.62 5745 CG2 VAL A 852 29.530 11.124 33.192 1.00 17.86 5746 N ALA A 853 26.272 9.662 36.315 1.00 17.66 5747 CA ALA A 853 25.839 8.989 37.544 1.00 16.64 5748 C ALA A 853 25.511 7.540 37.210 1.00 17.67 5749 O ALA A 853 24.951 7.276 36.117 1.00 18.63 5750 CB ALA A 853 24.565 9.709 38.039 1.00 15.15 5751 N PHE A 854 25.863 6.606 38.068 1.00 16.51 5752 CA PHE A 854 25.701 5.180 37.832 1.00 17.75 5753 C PHE A 854 25.400 4.431 39.126 1.00 18.33 5754 O PHE A 854 25.573 4.950 40.251 1.00 19.36 5755 CB PHE A 854 26.922 4.577 37.103 1.00 18.03 5756 CG PHE A 854 28.266 4.665 37.791 1.00 18.64 5757 CD1 PHE A 854 28.705 3.655 38.635 1.00 19.06 5758 CD2 PHE A 854 29.117 5.734 37.569 1.00 18.31 5759 CE1 PHE A 854 29.952 3.745 39.251 1.00 17.32 5760 CE2 PHE A 854 30.366 5.799 38.148 1.00 17.33 5761 CZ PHE A 854 30.793 4.792 39.003 1.00 15.66 5762 N GLU A 855 24.837 3.226 38.985 1.00 18.41 5763 CA GLU A 855 24.385 2.432 40.134 1.00 18.15 5764 C GLU A 855 24.952 1.008 40.033 1.00 17.60 5765 O GLU A 855 25.011 0.485 38.900 1.00 15.72 5766 CB GLU A 855 22.839 2.373 40.213 1.00 17.57 5767 CG GLU A 855 22.296 1.628 41.437 1.00 18.25 5768 CD GLU A 855 20.756 1.617 41.583 1.00 21.29 5769 OE1 GLU A 855 20.194 1.168 42.603 1.00 18.85 5770 OE2 GLU A 855 20.095 2.079 40.611 1.00 22.94 5771 N LEU A 856 25.606 0.580 41.096 1.00 17.21 5772 CA LEU A 856 26.188 −0.794 41.188 1.00 18.95 5773 C LEU A 856 25.172 −1.634 41.962 1.00 18.66 5774 O LEU A 856 24.868 −1.303 43.156 1.00 20.65 5775 CB LEU A 856 27.582 −0.729 41.838 1.00 15.58 5776 CG LEU A 856 28.600 0.261 41.242 1.00 15.91 5777 CD1 LEU A 856 29.935 0.194 42.026 1.00 15.73 5778 CD2 LEU A 856 28.851 −0.034 39.762 1.00 15.55 5779 N LYS A 857 24.482 −2.559 41.308 1.00 20.01 5780 CA LYS A 857 23.349 −3.244 41.916 1.00 21.47 5781 C LYS A 857 23.415 −4.614 42.559 1.00 19.85 5782 O LYS A 857 24.129 −5.512 42.141 1.00 16.38 5783 CB LYS A 857 22.273 −3.433 40.784 1.00 23.29 5784 CG LYS A 857 21.724 −2.106 40.284 1.00 26.57 5785 CD LYS A 857 20.895 −2.342 38.990 1.00 28.26 5786 CE LYS A 857 21.874 −2.829 37.915 1.00 29.07 5787 NZ LYS A 857 21.301 −3.488 36.718 1.00 28.50 5788 N ASN A 858 22.551 −4.779 43.556 1.00 20.08 5789 CA ASN A 858 22.342 −6.017 44.296 1.00 22.03 5790 C ASN A 858 23.574 −6.787 44.771 1.00 19.15 5791 O ASN A 858 23.832 −7.961 44.451 1.00 17.47 5792 CB ASN A 858 21.481 −6.963 43.428 1.00 24.99 5793 CG ASN A 858 20.672 −7.932 44.294 1.00 27.08 5794 OD1 ASN A 858 20.308 −7.642 45.418 1.00 25.89 5795 ND2 ASN A 858 20.346 −9.104 43.726 1.00 28.26 5796 N TYR A 859 24.290 −6.198 45.719 1.00 15.00 5797 CA TYR A 859 25.524 −6.732 46.272 1.00 15.84 5798 C TYR A 859 26.470 −7.231 45.162 1.00 14.81 5799 O TYR A 859 26.871 −8.386 45.149 1.00 13.23 5800 CB TYR A 859 25.147 −7.865 47.215 1.00 17.53 5801 CG TYR A 859 24.243 −7.457 48.362 1.00 18.89 5802 CD1 TYR A 859 22.870 −7.641 48.244 1.00 20.51 5803 CD2 TYR A 859 24.719 −6.915 49.548 1.00 17.97 5804 CE1 TYR A 859 21.995 −7.319 49.262 1.00 20.07 5805 CE2 TYR A 859 23.860 −6.602 50.574 1.00 18.09 5806 CZ TYR A 859 22.496 −6.786 50.428 1.00 21.56 5807 OH TYR A 859 21.657 −6.473 51.472 1.00 20.57 5808 N ALA A 860 26.756 −6.405 44.195 1.00 14.63 5809 CA ALA A 860 27.573 −6.753 43.030 1.00 16.97 5810 C ALA A 860 28.955 −7.249 43.442 1.00 18.77 5811 O ALA A 860 29.597 −6.651 44.336 1.00 19.26 5812 CB ALA A 860 27.744 −5.511 42.164 1.00 18.48 5813 N ASN A 861 29.362 −8.365 42.860 1.00 18.35 5814 CA ASN A 861 30.655 −8.995 43.164 1.00 18.84 5815 C ASN A 861 30.855 −9.139 44.672 1.00 19.08 5816 O ASN A 861 31.935 −8.866 45.226 1.00 18.01 5817 CB ASN A 861 31.796 −8.205 42.485 1.00 18.52 5818 CG ASN A 861 33.144 −8.920 42.430 1.00 18.65 5819 OD1 ASN A 861 33.182 −10.129 42.202 1.00 18.09 5820 ND2 ASN A 861 34.255 −8.206 42.638 1.00 16.42 5821 N HIS A 862 29.923 −9.745 45.420 1.00 18.36 5822 CA HIS A 862 29.912 −10.026 46.835 1.00 18.01 5823 C HIS A 862 30.326 −8.786 47.655 1.00 18.23 5824 O HIS A 862 31.071 −8.845 48.634 1.00 19.60 5825 CB HIS A 862 30.725 −11.267 47.307 1.00 18.46 5826 CG HIS A 862 32.194 −11.226 46.999 1.00 20.04 5827 ND1 HIS A 862 32.690 −11.802 45.836 1.00 21.25 5828 CD2 HIS A 862 33.279 −10.659 47.560 1.00 21.51 5829 CE1 HIS A 862 33.983 −11.616 45.725 1.00 21.85 5830 NE2 HIS A 862 34.380 −10.896 46.767 1.00 23.07 5831 N ASP A 863 29.770 −7.637 47.354 1.00 16.12 5832 CA ASP A 863 29.883 −6.424 48.130 1.00 17.57 5833 C ASP A 861 28.980 −6.498 49.361 1.00 16.17 5834 O ASP A 863 27.999 −7.241 49.361 1.00 15.89 5835 CB ASP A 863 29.435 −5.250 47.242 1.00 17.41 5836 CG ASP A 863 30.045 −3.935 47.687 1.00 19.24 5837 OD1 ASP A 863 31.158 −3.597 47.207 1.00 15.53 5838 OD2 ASP A 863 29.459 −3.191 48.509 1.00 20.34 5839 N THR A 864 29.270 −5.700 50.388 1.00 16.93 5840 CA THR A 864 28.442 −5.615 51.570 1.00 17.66 5841 C THR A 864 27.315 −4.585 51.445 1.00 19.37 5842 O THR A 864 26.382 −4.558 52.256 1.00 19.59 5843 CB THR A 864 29.230 −5.242 52.846 1.00 18.03 5844 OG1 THR A 864 30.031 −4.081 52.545 1.00 18.52 5845 CG2 THR A 864 30.062 −6.428 53.337 1.00 17.90 5846 N TRP A 865 27.378 −3.754 50.419 1.00 18.22 5847 CA TRP A 865 26.366 −2.703 50.191 1.00 19.88 5848 C TRP A 865 25.478 −3.241 49.072 1.00 21.10 5849 O TRP A 865 25.965 −3.703 48.039 1.00 19.83 5850 CB TRP A 865 27.055 −1.385 49.870 1.00 20.11 5851 CG TRP A 865 27.697 −0.603 50.975 1.00 20.00 5852 CD1 TRP A 865 27.512 −0.899 52.310 1.00 20.46 5853 CD2 TRP A 865 28.490 0.608 50.952 1.00 19.16 5854 NE1 TRP A 865 28.207 −0.016 53.072 1.00 19.59 5855 CE2 TRP A 865 28.808 0.918 52.281 1.00 20.04 5856 CE3 TRP A 865 29.016 1.392 49.936 1.00 18.40 5857 CZ2 TRP A 865 29.584 2.019 52.639 1.00 19.58 5858 CZ3 TRP A 865 29.777 2.502 50.287 1.00 20.06 5859 CH2 TRP A 865 30.082 2.782 51.624 1.00 18.82 5860 N LYS A 866 24.171 −3.257 49.278 1.00 18.45 5861 CA LYS A 866 23.184 −3.732 48.319 1.00 20.04 5862 C LYS A 866 23.133 −2.967 47.004 1.00 19.12 5863 O LYS A 866 23.316 −3.533 45.926 1.00 16.36 5864 CB LYS A 866 21.813 −3.689 49.002 1.00 20.69 5865 CG LYS A 866 20.635 −4.165 48.181 1.00 25.35 5866 CD LYS A 866 19.462 −4.533 49.094 1.00 30.56 5867 CE LYS A 866 18.162 −4.133 48.385 1.00 32.55 5868 NZ LYS A 866 17.703 −5.263 47.516 1.00 36.93 5869 N ASN A 867 22.957 −1.640 47.085 1.00 17.81 5870 CA ASN A 867 22.992 −0.817 45.878 1.00 19.57 5871 C ASN A 867 23.954 0.339 46.119 1.00 19.05 5872 O ASN A 867 23.947 0.830 47.255 1.00 17.99 5873 CB ASN A 867 21.656 −0.244 45.428 1.00 19.15 5874 CG ASN A 867 20.650 −1.322 45.045 1.00 20.68 5875 OD1 ASN A 867 20.987 −2.249 44.295 1.00 20.32 5876 ND2 ASN A 867 19.422 −1.255 45.549 1.00 17.97 5877 N ILE A 868 24.751 0.805 45.213 1.00 18.06 5878 CA ILE A 868 25.644 1.902 45.360 1.00 17.77 5879 C ILE A 868 25.425 2.872 44.217 1.00 17.69 5880 O ILE A 868 25.330 2.391 43.094 1.00 18.10 5881 CB ILE A 868 27.127 1.424 45.318 1.00 18.75 5882 CG1 ILE A 868 27.433 0.426 46.467 1.00 19.10 5883 CG2 ILE A 868 28.041 2.639 45.602 1.00 18.17 5884 CD1 ILE A 868 28.866 −0.183 46.382 1.00 19.08 5885 N ILE A 869 25.397 4.154 44.510 1.00 16.22 5886 CA ILE A 869 25.256 5.150 43.447 1.00 15.16 5887 C ILE A 869 26.496 6.039 43.528 1.00 15.96 5888 O ILE A 869 26.936 6.380 44.637 1.00 17.68 5889 CB ILE A 869 23.932 5.949 43.590 1.00 14.79 5890 CG1 ILE A 869 22.753 5.177 43.024 1.00 16.18 5891 CG2 ILE A 869 24.060 7.342 42.951 1.00 14.77 5892 CD1 ILE A 869 21.309 5.688 43.251 1.00 17.74 5893 N VAL A 870 27.084 6.345 42.385 1.00 13.11 5894 CA VAL A 870 28.208 7.276 42.308 1.00 15.88 5895 C VAL A 870 27.777 8.403 41.357 1.00 13.78 5896 O VAL A 870 27.303 8.071 40.277 1.00 14.36 5897 CB VAL A 870 29.500 6.597 41.787 1.00 16.19 5898 CG1 VAL A 870 30.634 7.584 41.464 1.00 17.02 5899 CG2 VAL A 870 29.989 5.575 42.845 1.00 15.31 5900 N MET A 871 28.093 9.657 41.556 1.00 15.32 5901 CA MET A 871 27.849 10.659 40.508 1.00 16.32 5902 C MET A 871 28.985 11.671 40.520 1.00 16.77 5903 O MET A 871 29.341 12.115 41.624 1.00 16.61 5904 CB MET A 871 26.511 11.402 40.645 1.00 17.18 5905 CG MET A 871 26.303 12.711 39.875 1.00 18.06 5906 SD MET A 871 24.576 13.307 40.042 1.00 17.89 5907 CE MET A 871 24.717 14.958 39.345 1.00 17.65 5908 N TYR A 872 29.496 11.964 39.333 1.00 15.67 5909 CA TYR A 872 30.520 13.001 39.181 1.00 17.64 5910 C TYR A 872 29.866 14.313 38.765 1.00 17.57 5911 O TYR A 872 29.125 14.271 37.786 1.00 18.01 5912 CB TYR A 872 31.569 12.699 38.081 1.00 16.70 5913 CG TYR A 872 32.156 11.318 38.208 1.00 16.28 5914 CD1 TYR A 872 32.120 10.472 37.110 1.00 13.82 5915 CD2 TYR A 872 32.651 10.833 39.432 1.00 17.04 5916 CE1 TYR A 872 32.631 9.180 37.193 1.00 15.56 5917 CE2 TYR A 872 33.138 9.522 39.527 1.00 15.23 5918 CZ TYR A 872 33.069 8.696 38.405 1.00 16.02 5919 OH TYR A 872 33.528 7.402 38.433 1.00 16.10 5920 N ASN A 873 30.114 15.425 39.416 1.00 18.25 5921 CA ASN A 873 29.599 16.720 39.021 1.00 17.41 5922 C ASN A 873 30.804 17.644 38.874 1.00 17.53 5923 O ASN A 873 31.181 18.240 39.867 1.90 18.67 5924 CB ASN A 873 28.650 17.362 40.055 1.00 18.79 5925 CG ASN A 873 28.169 18.759 39.681 1.00 19.71 5926 OD1 ASN A 873 28.219 19.179 38.513 1.00 19.99 5927 ND2 ASN A 873 27.768 19.612 40.630 1.00 16.40 5928 N PRO A 874 31.324 17.850 37.673 1.00 17.92 5929 CA PRO A 874 32.426 18.758 37.448 1.00 18.85 5930 C PRO A 874 31.964 20.201 37.260 1.00 20.43 5931 O PRO A 874 32.857 21.062 37.114 1.00 19.83 5932 CB PRO A 874 33.028 18.250 36.120 1.00 18.54 5933 CG PRO A 874 31.814 17.776 35.350 1.00 18.34 5934 CD PRO A 874 30.927 17.154 36.432 1.00 18.38 5935 N ASN A 875 30.658 20.487 37.266 1.00 18.81 5936 CA ASN A 875 30.197 21.862 37.056 1.00 21.71 5937 C ASN A 875 30.401 22.836 38.198 1.00 21.33 5938 O ASN A 875 30.422 22.397 39.369 1.00 20.55 5939 CB ASN A 878 28.687 21.786 36.701 1.00 22.52 5940 CG ASN A 875 28.451 20.853 35.519 1.00 24.12 5941 OD1 ASN A 875 28.894 21.182 34.417 1.00 26.00 5942 ND2 ASN A 875 27.799 19.711 35.664 1.00 21.36 5943 N LYS A 876 30.486 24.146 37.974 1.00 21.86 5944 CA LYS A 876 30.645 25.159 39.028 1.00 25.54 5945 C LYS A 876 29.380 25.447 39.861 1.00 23.68 5946 O LYS A 876 29.408 26.291 40.768 1.00 20.96 5947 CB LYS A 876 31.049 26.536 38.435 1.00 28.74 5948 CG LYS A 876 32.446 26.518 37.768 1.00 32.96 5949 CD LYS A 876 33.382 26.138 38.926 1.00 35.88 5950 CE LYS A 876 34.570 27.098 39.033 1.00 37.37 5951 NZ LYS A 876 35.469 26.778 37.875 1.00 36.83 5952 N THR A 877 28.261 24.779 39.591 1.00 22.70 5953 CA THR A 877 27.057 24.946 40.425 1.00 22.49 5954 C THR A 877 26.579 23.547 40.821 1.00 21.81 5955 O THR A 877 26.865 22.555 40.163 1.00 19.74 5956 CB THR A 877 25.891 25.589 39.673 1.00 22.36 5957 OG1 THR A 877 25.632 24.830 38.499 1.00 23.54 5958 CG2 THR A 877 26.212 27.030 39.271 1.00 25.23 5959 N SER A 878 25.857 23.541 41.955 1.00 18.08 5960 CA SER A 878 25.326 22.269 42.406 1.00 18.86 5961 C SER A 878 24.284 21.737 41.420 1.00 19.86 5962 O SER A 878 23.661 22.481 40.673 1.00 18.20 5963 CB SER A 878 24.366 22.598 43.617 1.00 16.87 5964 OG SER A 878 23.469 23.709 43.603 1.00 20.00 5965 N GLN A 879 24.144 20.400 41.475 1.00 20.32 5966 CA GLN A 879 23.180 19.790 40.580 1.00 21.86 5967 C GLN A 879 22.200 18.733 41.224 1.00 22.97 5968 O GLN A 879 22.675 18.029 42.131 1.00 21.65 5969 CB GLN A 879 23.931 18.974 39.468 1.00 22.37 5970 CG GLN A 879 24.910 19.802 38.645 1.00 22.60 5971 CD GLN A 879 24.240 20.815 37.750 1.00 23.49 5972 OE1 GLN A 879 23.305 20.445 37.029 1.00 24.49 5973 NE2 GLN A 879 24.740 22.035 37.686 1.00 23.81 5974 N THR A 880 20.980 18.539 40.721 1.00 20.70 5975 CA THR A 880 20.040 17.652 41.394 1.00 21.62 5976 C THR A 880 19.919 16.302 46.713 1.00 18.77 5977 O THR A 880 19.923 16.258 39.513 1.00 18.27 5978 CB THR A 880 18.613 18.275 41.489 1.00 25.07 5979 OG1 THR A 880 18.717 19.445 42.338 1.00 27.52 5980 CG2 THR A 880 17.672 17.294 42.200 1.00 26.46 5981 N LEU A 881 20.041 15.196 41.424 1.00 17.50 5982 CA LEU A 881 19.883 13.866 40.872 1.00 17.31 5983 C LEU A 881 18.575 13.262 41.401 1.00 17.89 5984 O LEU A 881 18.363 13.335 42.617 1.00 17.14 5985 CB LEU A 881 21.088 12.982 41.365 1.00 18.29 5986 CG LEU A 881 21.001 11.492 41.039 1.00 20.54 5987 CD1 LEU A 881 21.214 11.306 39.528 1.00 21.58 5988 CD2 LEU A 881 22.087 10.699 41.817 1.00 20.54 5989 N ASN A 882 17.745 12.668 40.578 1.00 18.74 5990 CA ASN A 882 16.529 11.983 40.974 1.00 20.32 5991 C ASN A 882 16.916 10.547 41.262 1.00 19.51 5992 O ASN A 882 17.686 9.944 40.505 1.00 21.26 5993 CB ASN A 882 15.547 12.040 39.832 1.00 24.52 5994 CG ASN A 882 15.024 13.451 39.705 1.00 27.48 5995 OD1 ASN A 882 14.600 14.087 40.666 1.00 28.76 5996 ND2 ASN A 882 15.063 13.946 38.456 1.00 20.00 5997 N LEU A 883 16.404 9.998 42.341 1.00 20.69 5998 CA LEU A 883 16.795 8.686 42.799 1.00 19.88 5999 C LEU A 883 15.783 7.565 42.619 1.00 21.80 6000 O LEU A 883 14.583 7.773 42.723 1.00 23.04 6001 CB LEU A 883 17.076 8.771 44.330 1.00 19.20 6002 CG LEU A 883 18.161 9.773 44.743 1.00 19.84 6003 CD1 LEU A 883 18.166 10.045 46.259 1.00 20.56 6004 CD2 LEU A 883 19.510 9.241 44.291 1.00 15.99 6005 N PRO A 884 16.303 6.364 42.482 1.00 20.55 6006 CA PRO A 884 15.498 5.168 42.474 1.00 23.11 6007 C PRO A 884 14.757 5.106 43.809 1.00 22.93 6008 O PRO A 884 15.119 5.780 44.796 1.00 21.23 6009 CB PRO A 884 16.530 4.053 42.301 1.00 22.91 6010 CG PRO A 884 17.714 4.713 41.660 1.00 21.54 6011 CD PRO A 884 17.762 6.046 42.397 1.00 20.96 6012 N SER A 885 13.760 4.240 43.934 1.00 21.66 6013 CA SER A 885 12.967 4.273 45.162 1.00 24.40 6014 C SER A 885 13.716 3.881 46.431 1.00 23.95 6015 O SER A 885 14.814 3.285 46.467 1.00 21.34 6016 CB SER A 885 11.706 3.395 44.996 1.00 25.34 6017 OG SER A 885 12.206 2.088 45.063 1.00 26.34 6018 N GLY A 886 13.117 4.365 47.544 1.00 21.95 6019 CA GLY A 886 13.647 3.960 48.850 1.00 21.89 6020 C GLY A 886 14.483 4.998 49.573 1.00 22.67 6021 O GLY A 886 14.689 6.146 49.165 1.00 23.42 6022 N ASP A 887 14.869 4.680 50.801 1.00 21.05 6023 CA ASP A 887 15.760 5.451 51.645 1.00 22.50 6024 C ASP A 887 17.214 5.281 51.210 1.00 20.68 6025 O ASP A 887 17.634 4.130 51.040 1.00 19.39 6026 CB ASP A 887 15.602 4.969 53.086 1.00 23.02 6027 CG ASP A 887 16.484 5.799 54.001 1.00 25.67 6028 OD1 ASP A 887 17.638 5.419 54.199 1.00 28.60 6029 OD2 ASP A 887 16.009 6.815 54.502 1.00 20.00 6030 N TRP A 888 17.977 6.376 51.081 1.00 19.72 6031 CA TRP A 888 19.375 6.298 50.691 1.00 17.29 6032 C TRP A 888 20.292 6.887 51.745 1.00 18.92 6033 O TRP A 888 19.985 7.977 52.265 1.00 19.35 6034 CB TRP A 888 19.584 6.970 49.305 1.00 19.14 6035 CG TRP A 888 19.041 6.188 48.135 1.00 21.37 6036 CD1 TRP A 888 17.777 6.307 47.614 1.00 19.94 6037 CD2 TRP A 888 19.692 5.196 47.325 1.00 23.02 6038 NE1 TRP A 888 17.616 5.449 46.549 1.00 20.33 6039 CE2 TRP A 888 18.775 4.742 46.365 1.00 21.10 6040 CE3 TRP A 888 20.966 4.626 47.345 1.00 23.66 6041 CZ2 TRP A 888 19.060 3.727 45.435 1.00 20.78 6042 CZ3 TRP A 888 21.271 3.645 46.396 1.00 23.95 6043 CH2 TRP A 888 20.330 3.181 45.469 1.00 21.41 6044 N THR A 889 21.444 6.290 52.074 1.00 16.86 6045 CA THR A 889 22.397 6.862 53.008 1.00 17.70 6046 C THR A 889 23.506 7.623 52.293 1.00 18.48 6047 O THR A 889 24.068 7.059 51.330 1.00 17.19 6048 CB THR A 889 23.071 5.754 53.870 1.00 18.89 6049 OG1 THR A 889 22.031 5.014 54.495 1.00 19.06 6050 CG2 THR A 889 23.995 6.360 54.928 1.00 16.36 6051 N ILE A 890 23.827 8.864 52.643 1.00 17.13 6052 CA ILE A 890 24.908 9.575 51.956 1.00 18.82 6053 C ILE A 890 26.259 9.160 52.591 1.00 18.09 6054 O ILE A 890 26.349 9.198 53.816 1.00 18.88 6055 CB ILE A 890 24.732 11.089 52.093 1.00 18.96 6056 CG1 ILE A 890 23.367 14.573 51.535 1.00 19.44 6057 CG2 ILE A 890 25.920 11.771 51.420 1.00 15.34 6058 CD1 ILE A 890 23.069 12.988 52.057 1.00 19.01 6059 N VAL A 891 27.241 8.700 51.844 1.00 17.95 6060 CA VAL A 891 28.536 8.307 52.362 1.00 17.49 6061 C VAL A 891 29.719 9.089 51.748 1.00 17.57 6062 O VAL A 891 30.808 9.192 52.354 1.00 16.92 6063 CB VAL A 891 28.904 6.821 52.307 1.00 18.15 6064 CG1 VAL A 891 27.983 6.048 53.233 1.00 19.10 6065 CG2 VAL A 891 28.997 6.205 50.921 1.00 18.18 6066 N GLY A 892 29.413 9.810 50.684 1.00 14.68 6067 CA GLY A 892 30.419 10.659 50.046 1.00 15.77 6068 C GLY A 892 29.792 12.007 49.641 1.00 18.34 6069 O GLY A 892 28.876 11.911 48.821 1.00 15.50 6070 N LEU A 893 30.225 13.102 50.237 1.00 17.98 6071 CA LEU A 893 29.668 14.397 49.870 1.00 18.16 6072 C LEU A 893 30.721 15.469 50.156 1.00 18.84 6073 O LEU A 893 31.329 15.577 51.225 1.00 18.84 6074 CB LEU A 893 28.353 14.725 50.598 1.00 18.93 6075 CG LEU A 893 27.657 16.052 50.223 1.00 20.31 6076 CD1 LEU A 893 26.160 15.915 50.545 1.00 19.83 6077 CD2 LEU A 893 28.199 17.314 50.895 1.00 19.07 6078 N GLY A 894 30.863 16.384 49.199 1.00 18.44 6079 CA GLY A 894 31.780 17.536 49.376 1.00 19.33 6080 C GLY A 894 33.173 16.936 49.592 1.00 21.53 6081 O GLY A 894 33.534 16.015 48.857 1.00 20.54 6082 N ASP A 895 33.906 17.393 50.605 1.00 20.89 6083 CA ASP A 895 35.240 16.835 50.842 1.00 22.34 6084 C ASP A 895 35.191 15.680 51.834 1.00 22.18 6085 O ASP A 895 36.127 15.514 52.615 1.00 24.94 6086 CB ASP A 895 36.130 17.947 51.393 1.00 22.12 6087 CG ASP A 895 35.478 18.553 52.622 1.00 23.64 6088 OD1 ASP A 895 36.022 19.522 53.153 1.00 25.64 6089 OD2 ASP A 895 34.435 18.052 53.033 1.00 20.00 6090 N GLN A 896 34.086 14.968 51.966 1.00 22.81 6091 CA GLN A 896 33.930 13.925 52.976 1.00 22.65 6092 C GLN A 896 33.662 12.612 52.237 1.00 22.28 6093 O GLN A 896 32.744 12.496 51.436 1.00 19.57 6094 CB GLN A 896 32.781 14.173 53.958 1.00 24.18 6095 CG GLN A 896 32.835 15.288 54.933 1.00 28.13 6096 CD GLN A 896 32.024 15.444 56.200 1.00 30.70 6097 OE1 GLN A 896 32.333 15.046 57.385 1.00 31.20 6098 NE2 GLN A 896 30.906 16.146 56.043 1.00 23.23 6099 N ILE A 897 34.546 11.646 52.545 1.00 20.05 6100 CA ILE A 897 34.366 10.348 51.925 1.00 19.25 6101 C ILE A 897 34.674 9.206 53.003 1.00 17.61 6102 O ILE A 897 35.565 9.391 53.822 1.00 17.24 6103 CB ILE A 897 35.364 9.778 50.777 1.00 21.18 6104 CG1 ILE A 897 35.494 11.058 49.949 1.00 19.62 6105 CG2 ILE A 897 34.751 8.692 49.874 1.00 24.68 6106 CD1 ILE A 897 34.203 10.877 49.148 1.00 20.00 6107 N GLY A 898 33.824 8.166 53.012 1.00 18.75 6108 CA GLY A 898 34.047 7.122 53.993 1.00 19.72 6109 C GLY A 898 32.917 6.112 54.045 1.00 21.21 6110 O GLY A 898 32.131 6.024 53.098 1.00 22.52 6111 N GLU A 899 32.839 5.374 55.134 1.00 22.66 6112 CA GLU A 899 31.848 4.331 55.295 1.00 24.68 6113 C GLU A 899 30.672 4.756 56.173 1.00 25.01 6114 O GLU A 899 29.690 4.011 56.229 1.00 25.22 6115 CB GLU A 899 32.539 3.087 55.883 1.00 25.95 6116 CG GLU A 899 33.810 2.569 55.207 1.00 25.09 6117 CD GLU A 899 33.525 1.712 53.981 1.00 25.77 6118 OE1 GLU A 899 32.401 1.155 53.967 1.00 25.14 6119 OE2 GLU A 899 34.413 1.517 53.062 1.00 24.44 6120 N LYS A 900 30.700 5.917 56.818 1.00 26.68 6121 CA LYS A 900 29.588 6.315 57.712 1.00 27.25 6122 C LYS A 900 28.562 7.272 57.137 1.00 25.12 6123 O LYS A 900 28.877 8.021 56.214 1.00 24.34 6124 CB LYS A 900 30.138 6.954 58.991 1.00 30.47 6125 CG LYS A 900 31.166 8.056 58.815 1.00 34.16 6126 CD LYS A 900 31.252 8.901 60.073 1.00 37.55 6127 CE LYS A 900 32.148 10.117 60.043 1.00 39.40 6128 NZ LYS A 900 31.814 11.176 59.022 1.00 39.28 6129 N SER A 901 27.347 7.305 57.686 1.00 22.18 6130 CA SER A 901 26.272 8.150 57.221 1.00 19.86 6131 C SER A 901 26.602 9.636 57.424 1.00 20.90 6132 O SER A 901 26.916 10.105 58.520 1.00 17.48 6133 CB SER A 901 24.943 7.837 57.959 1.00 20.68 6134 OG SER A 901 23.889 8.727 57.561 1.00 20.53 6135 N LEU A 902 26.313 10.398 56.397 1.00 20.11 6136 CA LEU A 902 26.356 11.850 56.363 1.00 21.86 6137 C LEU A 902 24.905 12.352 56.257 1.00 21.44 6138 O LEU A 902 24.619 13.483 55.884 1.00 23.50 6139 CB LEU A 902 27.161 12.292 55.123 1.00 20.45 6140 CG LEU A 902 28.648 11.907 55.124 1.00 21.85 6141 CD1 LEU A 902 29.313 12.215 53.787 1.00 21.36 6142 CD2 LEU A 902 29.429 12.647 56.213 1.00 23.54 6143 N GLY A 903 23.941 11.490 56.527 1.00 22.23 6144 CA GLY A 903 22.507 11.805 56.400 1.00 21.35 6145 C GLY A 903 21.755 10.820 55.503 1.00 22.85 6146 O GLY A 903 22.304 9.974 54.773 1.00 21.12 6147 N HIS A 904 20.416 10.897 55.544 1.00 21.69 6148 CA HIS A 904 19.535 10.011 54.797 1.00 23.46 6149 C HIS A 904 18.628 10.789 53.870 1.00 23.10 6150 O HIS A 904 18.198 11.869 54.301 1.00 24.57 6151 CB HIS A 904 18.698 9.166 55.765 1.00 24.48 6152 CG HIS A 904 19.422 8.024 56.402 1.00 25.51 6153 ND1 HIS A 904 20.109 8.146 57.599 1.00 26.84 6154 CD2 HIS A 904 19.509 6.720 56.060 1.00 25.70 6155 CE1 HIS A 904 20.654 6.968 57.906 1.00 24.89 6156 NE2 HIS A 904 20.287 6.092 57.025 1.00 26.58 6157 N VAL A 905 18.379 10.385 52.631 1.00 20.66 6158 CA VAL A 905 17.530 11.105 51.710 1.00 21.55 6159 C VAL A 905 16.686 10.142 50.856 1.00 22.40 6160 O VAL A 905 16.926 8.935 50.724 1.00 21.14 6161 CB VAL A 905 18.271 12.035 50.716 1.00 22.34 6162 CG1 VAL A 905 19.182 13.071 51.320 1.00 22.74 6163 CG2 VAL A 905 19.108 11.151 49.778 1.00 22.37 6164 N MET A 906 15.637 10.699 50.260 1.00 21.77 6165 CA MET A 906 14.755 9.959 49.363 1.00 24.07 6166 C MET A 906 14.160 10.924 48.328 1.00 23.61 6167 O MET A 906 14.031 12.130 48.524 1.00 22.79 6168 CB MET A 906 13.578 9.416 50.195 1.00 26.81 6169 CG MET A 906 12.397 10.208 50.760 1.00 32.84 6170 SD MET A 906 11.387 9.012 51.643 1.00 20.00 6171 CE MET A 906 11.948 7.311 51.468 1.00 20.00 6172 N GLY A 907 13.907 10.353 47.148 1.00 21.83 6173 CA GLY A 907 13.278 11.077 46.048 1.00 21.53 6174 C GLY A 907 14.374 11.725 45.200 1.00 20.44 6175 O GLY A 907 14.554 11.417 44.029 1.00 18.16 6176 N ASN A 908 15.070 12.662 45.868 1.00 20.78 6177 CA ASN A 908 16.156 13.320 45.167 1.00 21.15 6178 C ASN A 908 17.211 13.868 46.130 1.00 20.98 6179 O ASN A 908 17.017 13.926 47.338 1.00 18.52 6180 CB ASN A 908 15.571 14.503 44.390 1.00 25.44 6181 CG ASN A 908 15.149 15.737 45.145 1.00 20.00 6182 OD1 ASN A 908 14.950 16.900 44.807 1.00 20.00 6183 ND2 ASN A 908 14.852 15.267 46.369 1.00 20.00 6184 N VAL A 909 18.336 14.263 45.507 1.00 18.91 6185 CA VAL A 909 19.404 14.800 46.327 1.00 18.32 6186 C VAL A 909 20.288 15.881 45.643 1.00 18.88 6187 O VAL A 909 20.470 15.801 44.414 1.00 16.18 6188 CB VAL A 909 20.296 13.598 46.765 1.00 17.97 6189 CG1 VAL A 909 20.923 12.911 45.546 1.00 19.38 6190 CG2 VAL A 909 21.470 13.978 47.699 1.00 17.98 6191 N GLN A 910 20.764 16.892 46.388 1.00 17.12 6192 CA GLN A 910 21.594 17.918 45.745 1.00 19.67 6193 C GLN A 910 23.093 17.606 45.891 1.00 20.86 6194 O GLN A 910 23.536 17.338 47.015 1.00 17.07 6195 CB GLN A 910 21.229 19.312 46.287 1.00 22.85 6196 CG GLN A 910 19.856 19.985 46.266 1.00 27.05 6197 CD GLN A 910 19.701 21.417 46.720 1.00 30.96 6198 OE1 GLN A 910 20.065 22.155 45.819 1.00 34.28 6199 NE2 GLN A 910 19.496 21.840 47.984 1.00 20.00 6200 N VAL A 911 23.796 17.686 44.736 1.00 19.28 6201 CA VAL A 911 25.245 17.405 44.720 1.00 17.62 6202 C VAL A 911 26.083 18.669 44.564 1.00 16.72 6203 O VAL A 911 25.929 19.417 43.604 1.00 15.75 6204 CB VAL A 911 25.554 16.486 43.522 1.00 18.06 6205 CG1 VAL A 911 27.073 16.218 43.441 1.00 17.92 6206 CG2 VAL A 911 24.732 15.197 43.636 1.00 17.78 6207 N PRO A 912 27.026 18.916 45.461 1.00 16.38 6208 CA PRO A 912 27.871 20.082 45.470 1.00 17.42 6209 C PRO A 912 28.675 20.351 44.198 1.00 18.48 6210 O PRO A 912 29.107 19.443 43.466 1.00 16.06 6211 CB PRO A 912 28.858 19.807 46.625 1.00 18.95 6212 CG PRO A 912 28.014 19.010 47.577 1.00 18.32 6213 CD PRO A 912 27.262 18.053 46.667 1.00 17.58 6214 N ALA A 913 28.947 21.637 43.934 1.00 18.47 6215 CA ALA A 913 29.792 21.934 42.707 1.00 18.97 6216 C ALA A 913 31.156 21.235 42.809 1.00 19.12 6217 O ALA A 913 31.887 21.154 43.805 1.00 18.44 6218 CB ALA A 913 30.037 23.434 42.685 1.00 19.77 6219 N ILE A 914 31.633 20.856 41.633 1.00 18.72 6220 CA ILE A 914 32.920 20.212 41.447 1.00 19.25 6221 C ILE A 914 33.188 19.086 42.437 1.00 17.77 6222 O ILE A 914 34.174 19.116 43.194 1.00 14.80 6223 CB ILE A 914 34.148 21.132 41.309 1.00 23.32 6224 CG1 ILE A 914 34.131 22.434 40.505 1.00 20.00 6225 CG2 ILE A 914 35.175 20.189 43.657 1.00 20.00 6226 CD1 ILE A 914 35.357 23.346 40.425 1.00 27.60 6227 N SER A 915 32.382 18.019 42.461 1.00 16.85 6228 CA SER A 915 32.568 16.964 43.470 1.00 17.87 6229 C SER A 915 31.956 15.634 43.080 1.00 16.66 6230 O SER A 915 31.365 15.476 42.014 1.00 16.70 6231 CB SER A 915 31.875 17.394 44.797 1.00 19.13 6232 OG SER A 915 30.465 17.164 44.596 1.00 18.25 6233 N THR A 916 32.324 14.578 43.799 1.00 15.50 6234 CA THR A 916 31.790 13.243 43.594 1.00 13.88 6235 C THR A 916 30.813 12.945 44.738 1.00 16.32 6236 O THR A 916 31.111 13.139 45.938 1.00 16.25 6237 CB THR A 916 32.932 12.214 43.565 1.00 15.91 6238 OG1 THR A 916 33.805 12.538 42.444 1.00 16.29 6239 CG2 THR A 916 32.413 10.796 43.465 1.00 15.30 6240 N LEU A 917 29.643 12.422 44.406 1.00 18.04 6241 CA LEU A 917 28.642 12.007 45.400 1.00 19.93 6242 C LEU A 917 28.612 10.487 45.449 1.00 18.73 6243 O LEU A 917 28.780 9.832 44.413 1.00 19.02 6244 CB LEU A 917 27.290 12.536 44.972 1.00 20.24 6245 CG LEU A 917 26.165 12.061 45.884 1.00 20.00 6246 CD1 LEU A 917 25.876 13.041 47.022 1.00 21.86 6247 CD2 LEU A 917 24.848 11.880 45.129 1.00 20.00 6248 N ILE A 918 28.502 9.935 46.675 1.00 16.06 6249 CA ILE A 918 28.452 8.487 46.780 1.00 16.89 6250 C ILE A 918 27.272 8.137 47.700 1.00 18.66 6251 O ILE A 918 27.097 8.663 48.785 1.00 16.20 6252 CB ILE A 918 29.732 7.784 47.268 1.00 17.77 6253 CG1 ILE A 918 30.930 8.148 46.370 1.00 18.54 6254 CG2 ILE A 918 29.487 6.275 47.309 1.00 17.76 6255 CD1 ILE A 918 32.249 7.494 46.754 1.00 20.20 6256 N LEU A 919 26.369 7.351 47.131 1.00 21.26 6257 CA LEU A 919 25.184 6.865 47.783 1.00 27.90 6258 C LEU A 919 25.295 5.346 47.929 1.00 30.33 6259 O LEU A 919 25.969 4.669 47.164 1.00 32.18 6260 CB LEU A 919 23.770 7.282 47.400 1.00 25.84 6261 CG LEU A 919 23.523 8.755 47.030 1.00 24.77 6262 CD1 LEU A 919 22.135 8.877 46.388 1.00 25.08 6263 CD2 LEU A 919 23.622 9.633 48.256 1.00 24.26 6264 N LYS A 920 24.551 4.859 48.938 1.00 36.42 6265 CA LYS A 920 24.617 3.434 49.196 1.00 43.04 6266 C LYS A 920 23.193 3.022 49.576 1.00 45.32 6267 1OCT LYS A 920 22.398 3.801 51.035 1.00 45.54 6268 CB LYS A 920 25.523 2.759 50.280 1.00 44.65 6269 CG LYS A 920 24.968 2.992 51.689 1.00 44.34 6270 CD LYS A 920 25.851 2.376 52.776 1.00 20.00 6271 CE LYS A 920 25.377 2.731 54.189 1.00 20.00 6272 NZ LYS A 920 25.874 1.739 55.139 1.00 20.00 6273 N GLN A 921 22.682 1.858 49.773 1.00 20.00 6274 CA GLN A 921 21.286 1.476 50.372 1.00 20.00 6275 C GLN A 921 21.261 0.073 50.618 1.00 20.00 6276 O GLN A 921 22.159 −0.710 50.334 1.00 20.00 6277 CB GLN A 921 19.846 1.531 49.828 1.00 20.00 6278 CG GLN A 921 19.352 2.234 48.564 1.00 20.00 6279 CD GLN A 921 18.079 1.727 47.929 1.00 20.00 6280 OE1 GLN A 921 17.783 0.808 47.183 1.00 20.00 6281 NE2 GLN A 921 17.165 2.459 48.597 1.00 20.00 6282 OW0 WAT W 68 69.366 −6.548 12.439 1.00 14.02 6283 OW0 WAT W 69 32.120 −4.756 50.871 1.00 13.28 6284 OW0 WAT W 70 81.609 −10.422 31.503 1.00 15.09 6285 OW0 WAT W 71 62.367 −0.879 37.668 1.00 12.62 6286 OW0 WAT W 73 68.913 −12.263 29.623 1.00 13.17 6287 OW0 WAT W 74 48.063 10.500 38.858 1.00 11.72 6288 OW0 WAT W 75 32.559 −7.482 50.485 1.00 13.66 6289 OW0 WAT W 76 32.469 1.638 38.626 1.00 14.80 6290 OW0 WAT W 77 65.428 −1.416 31.925 1.00 11.95 6291 OW0 WAT W 78 48.212 16.412 42.613 1.00 20.28 6292 OW0 WAT W 79 57.789 3.719 36.390 1.00 12.67 6293 OW0 WAT W 80 75.360 −12.767 22.439 1.00 15.67 6294 OW0 WAT W 81 61.875 −3.084 20.619 1.00 17.60 6295 OW0 WAT W 82 60.223 −2.292 27.508 1.00 11.71 6296 OW0 WAT W 83 73.802 −6.472 17.967 1.00 11.91 6297 OW0 WAT W 84 63.768 4.437 40.319 1.00 13.88 6298 OW0 WAT W 85 36.975 5.299 53.420 1.00 17.10 6299 OW0 WAT W 86 33.546 14.270 46.569 1.00 19.57 6300 OW0 WAT W 87 59.158 9.717 41.808 1.00 15.61 6301 OW0 WAT W 88 41.880 −1.805 42.672 1.00 18.22 6302 OW0 WAT W 89 56.275 9.738 41.533 1.00 13.72 6303 OW0 WAT W 99 69.059 −23.930 9.758 1.00 20.01 6304 OW0 WAT W 91 16.344 1.857 52.326 1.00 22.62 6305 OW0 WAT W 92 75.875 −9.053 49.382 1.00 20.09 6306 OW0 WAT W 93 76.720 −4.117 4.820 1.00 19.57 6307 OW0 WAT W 94 32.604 16.958 29.686 1.00 15.11 6308 OW0 WAT W 95 14.139 7.588 47.083 1.00 18.86 6309 OW0 WAT W 96 39.342 −8.437 34.765 1.00 18.36 6310 OW0 WAT W 97 53.612 13.510 41.564 1.00 15.07 6311 OW0 WAT W 98 36.908 −3.575 37.657 1.00 16.19 6312 OW0 WAT W 99 81.997 −19.278 2.244 1.00 21.87 6313 OW0 WAT W 100 34.008 1.090 27.119 1.00 17.80 6314 OW0 WAT W 101 56.888 19.001 45.064 1.00 16.05 6315 OW0 WAT W 102 31.113 8.775 55.007 1.00 16.75 6316 OW0 WAT W 103 68.763 −13.614 32.213 1.00 14.83 6317 OW0 WAT W 104 77.576 −15.120 38.787 1.00 17.30 6318 OW0 WAT W 105 70.975 9.008 41.415 1.00 15.80 6319 OW0 WAT W 106 73.071 8.260 45.444 1.00 19.77 6320 OW0 WAT W 107 29.643 15.604 46.570 1.00 15.52 6321 OW0 WAT W 108 77.037 −3.080 44.844 1.00 17.45 6322 OW0 WAT W 109 71.489 −9.613 39.434 1.00 14.35 6323 OW0 WAT W 110 41.593 −4.442 45.963 1.00 18.94 6324 OW0 WAT W 111 63.736 −11.016 10.939 1.00 17.44 6325 OW0 WAT W 112 40.024 2.255 37.806 1.00 13.52 6326 OW0 WAT W 113 64.610 −1.339 34.837 1.00 14.96 6327 OW0 WAT W 114 61.987 20.548 50.028 1.00 19.83 6328 OW0 WAT W 115 72.528 −7.124 29.593 1.00 18.15 6329 OW0 WAT W 116 47.271 −11.141 34.789 1.00 18.03 6330 OW0 WAT W 117 50.553 17.125 41.460 1.00 18.99 6331 OW0 WAT W 118 54.956 14.273 35.671 1.00 17.04 6332 OW0 WAT W 119 22.721 16.885 49.692 1.00 18.22 6333 OW0 WAT W 120 68.820 9.178 39.628 1.00 15.40 6334 OW0 WAT W 121 58.258 13.263 29.566 1.00 17.29 6335 OW0 WAT W 122 51.860 −6.953 40.625 1.00 16.39 6336 OW0 WAT W 123 24.503 9.804 33.921 1.00 16.52 6337 OW0 WAT W 124 82.641 −4.698 41.936 1.00 23.28 6338 OW0 WAT W 125 81.955 −8.160 8.351 1.00 24.39 6339 OW0 WAT W 126 62.535 5.308 26.770 1.00 21.48 6340 OW0 WAT W 127 46.588 −10.586 39.440 1.00 17.61 6341 OW0 WAT W 128 60.874 11.097 38.475 1.00 15.05 6342 OW0 WAT W 129 79.219 −10.342 12.004 1.00 17.14 6343 OW0 WAT W 130 75.096 −14.661 24.693 1.00 15.31 6344 OW0 WAT W 131 37.686 29.364 40.600 1.00 21.16 6345 OW0 WAT W 132 67.581 0.034 15.638 1.00 16.05 6346 OW0 WAT W 133 70.269 1.088 49.178 1.00 14.16 6347 OW0 WAT W 134 77.523 −12.820 37.177 1.00 13.66 6348 OW0 WAT W 135 77.079 −2.476 26.781 1.00 22.54 6349 OW0 WAT W 136 44.250 −9.198 31.555 1.00 19.30 6350 OW0 WAT W 137 43.079 26.840 29.301 1.00 23.07 6351 OW0 WAT W 138 73.331 −7.883 32.692 1.00 14.37 6352 OW0 WAT W 139 70.346 8.134 44.604 1.00 19.57 6353 OW0 WAT W 148 47.819 9.959 23.729 1.00 19.80 6354 OW0 WAT W 141 48.447 −8.906 33.755 1.00 15.32 6355 OW0 WAT W 142 29.592 15.853 27.070 1.00 25.10 6356 OW0 WAT W 143 45.897 −14.006 −16.368 1.00 21.95 6357 OW0 WAT W 144 65.522 5.063 38.083 1.00 12.12 6358 OW0 WAT W 145 67.211 0.550 32.731 1.00 17.01 6359 OW0 WAT W 146 58.188 15.032 33.459 1.00 18.00 6360 OW0 WAT W 147 56.888 −10.260 18.807 1.00 24.03 6361 OW0 WAT W 148 69.862 −15.067 24.194 1.00 12.26 6362 OW0 WAT W 149 66.848 18.769 50.441 1.00 26.40 6363 OW0 WAT W 150 39.850 10.596 24.937 1.00 15.47 6364 OW0 WAT W 151 46.212 −0.290 −4.537 1.00 19.55 6365 OW0 WAT W 152 69.349 10.471 29.638 1.00 25.61 6368 OW0 WAT W 153 75.556 −7.180 31.034 1.00 17.73 6367 OW0 WAT W 154 77.494 −24.179 15.886 1.00 19.43 6368 OW0 WAT W 155 62.259 12.967 49.436 1.00 16.99 6369 OW0 WAT W 157 81.536 −10.906 5.685 1.00 17.76 6370 OW0 WAT W 158 62.854 −16.944 21.280 1.00 30.32 6371 OW0 WAT W 159 47.815 −3.762 −20.195 1.00 24.16 6372 OW0 WAT W 160 74.332 −2.627 26.574 1.00 20.89 6373 OW0 WAT W 161 73.134 −8.343 11.701 1.00 14.37 6374 OW0 WAT W 162 35.562 −10.370 30.256 1.00 16.76 6375 OW0 WAT W 163 89.451 −13.445 20.007 1.00 17.74 6376 OW0 WAT W 164 64.437 −8.353 11.350 1.00 19.87 6377 OW0 WAT W 165 42.448 −1.014 52.692 1.00 25.22 6378 OW0 WAT W 166 46.191 −7.466 32.597 1.00 19.58 6379 OW0 WAT W 167 74.558 −4.139 51.689 1.00 21.48 6380 OW0 WAT W 168 58.356 12.098 38.036 1.00 18.33 6381 OW0 WAT W 169 64.827 20.010 32.662 1.00 24.95 6382 OW0 WAT W 170 46.993 18.543 20.841 1.00 20.41 6383 OW0 WAT W 171 36.631 21.698 36.640 1.00 16.69 6384 OW0 WAT W 172 54.527 4.577 34.040 1.00 16.16 6385 OW0 WAT W 173 79.048 −13.312 16.275 1.00 19.28 6386 OW0 WAT W 174 34.755 5.781 57.522 1.00 28.62 6387 OW0 WAT W 175 24.290 −8.263 41.358 1.00 27.30 6388 OW0 WAT W 176 43.005 20.391 32.602 1.00 20.84 6389 OW0 WAT W 177 30.870 −2.649 54.736 1.00 25.48 6390 OW0 WAT W 178 53.261 8.959 50.601 1.00 24.03 6391 OW0 WAT W 179 53.517 5.558 31.784 1.00 24.92 6392 OW0 WAT W 180 68.153 −15.586 16.468 1.00 17.73 6393 OW0 WAT W 181 80.333 −14.549 −8.414 1.00 28.75 6394 OW0 WAT W 182 77.155 4.046 42.470 1.00 16.63 6395 OW0 WAT W 183 36.194 17.220 43.863 1.00 17.32 6396 OW0 WAT W 184 74.883 3.842 36.300 1.00 18.34 6397 OW0 WAT W 185 43.383 31.022 45.350 1.00 34.65 6398 OW0 WAT W 186 55.792 6.996 60.761 1.00 19.70 6399 OW0 WAT W 187 62.221 10.100 60.967 1.00 17.41 6400 OW0 WAT W 188 72.467 −14.137 23.905 1.00 18.11 6401 OW0 WAT W 189 43.775 −10.296 29.198 1.00 13.72 6402 OW0 WAT W 190 46.321 8.776 37.734 1.00 17.82 6403 OW0 WAT W 191 58.197 4.756 57.467 1.00 18.48 6404 OW0 WAT W 192 18.946 19.472 50.053 1.00 43.73 6405 OW0 WAT W 193 46.641 23.645 40.314 1.00 15.11 6406 OW0 WAT W 194 73.073 2.447 2.145 1.00 25.40 6407 OW0 WAT W 195 69.006 20.130 42.674 1.00 29.03 6408 OW0 WAT W 196 68.843 −18.109 15.825 1.00 22.65 6409 OW0 WAT W 197 18.045 9.415 37.687 1.00 23.22 6410 OW0 WAT W 198 19.821 3.539 53.564 1.00 25.47 6411 OW0 WAT W 199 37.934 −8.358 42.258 1.00 22.96 6412 OW0 WAT W 200 66.324 −17.028 33.133 1.00 21.67 6413 OW0 WAT W 201 89.568 −0.730 43.526 1.00 39.85 6414 OW0 WAT W 202 65.791 −8.953 56.239 1.00 24.77 6415 OW0 WAT W 203 30.336 −3.688 −15.714 1.00 31.23 6416 OW0 WAT W 204 38.412 2.069 31.675 1.00 14.46 6417 OW0 WAT W 205 48.840 −16.134 30.302 1.00 22.40 6418 OW0 WAT W 206 66.776 20.286 40.341 1.00 25.65 6419 OW0 WAT W 207 37.823 3.881 27.553 1.00 16.42 6420 OW0 WAT W 208 51.918 25.040 45.285 1.00 35.74 6421 OW0 WAT W 209 57.850 21.185 46.630 1.00 23.05 6422 OW0 WAT W 210 20.044 17.034 49.140 1.00 14.24 6423 OW0 WAT W 211 71.715 −5.894 10.737 1.00 16.38 6424 OW0 WAT W 212 66.725 −5.950 11.424 1.00 25.24 6425 OW0 WAT W 213 69.977 −19.080 28.620 1.00 22.47 6426 OW0 WAT W 214 41.220 −1.629 45.498 1.00 14.57 6427 OW0 WAT W 215 80.849 −10.168 9.676 1.00 15.11 6428 OW0 WAT W 216 65.460 −4.423 5.582 1.00 25.44 6429 OW0 WAT W 217 60.371 3.984 54.712 1.00 19.11 6430 OW0 WAT W 218 46.146 −14.480 −19.119 1.00 22.68 6431 OW0 WAT W 220 75.425 −5.678 28.718 1.00 14.44 6432 OW0 WAT W 221 64.613 5.872 48.455 1.00 15.74 6433 OW0 WAT W 222 76.468 4.175 45.089 1.00 15.34 6434 OW0 WAT W 223 78.530 −3.248 30.018 1.00 18.35 6435 OW0 WAT W 224 66.447 −15.601 45.227 1.00 21.57 6436 OW0 WAT W 225 64.601 13.864 43.344 1.00 19.79 6437 OW0 WAT W 226 84.129 −21.451 40.447 1.00 23.07 6438 OW0 WAT W 227 50.240 9.246 25.340 1.00 27.34 6439 OW0 WAT W 228 71.340 −3.838 2.003 1.00 28.41 6440 OW0 WAT W 229 85.282 −20.669 0.886 1.00 31.69 6441 OW0 WAT W 230 26.568 −10.850 46.117 1.00 21.74 6442 OW0 WAT W 231 70.878 −18.207 31.358 1.00 23.68 6443 OW0 WAT W 232 35.309 24.294 36.012 1.00 20.39 6444 OW0 WAT W 233 52.580 4.977 18.388 1.00 22.44 6445 OW0 WAT W 234 50.557 11.295 58.608 1.00 20.04 6446 OW0 WAT W 235 23.949 20.846 34.191 1.00 26.29 6447 OW0 WAT W 236 35.623 14.411 43.636 1.00 19.95 6448 OW0 WAT W 237 64.405 −7.438 8.777 1.00 24.16 6449 OW0 WAT W 238 75.076 −15.366 34.214 1.00 24.35 6450 OW0 WAT W 239 49.006 −14.858 26.445 1.00 18.45 6451 OW0 WAT W 240 67.130 18.121 47.777 1.00 26.38 6452 OW0 WAT W 241 58.462 −8.275 −6.771 1.00 27.46 6453 OW0 WAT W 242 89.032 −3.538 32.201 1.00 37.77 6454 OW0 WAT W 243 76.413 −9.886 12.043 1.00 19.59 6455 OW0 WAT W 244 91.058 −23.122 27.002 1.00 29.55 6456 OW0 WAT W 245 68.897 −16.420 32.353 1.00 17.73 6457 OW0 WAT W 246 60.787 20.118 45.579 1.00 19.06 6458 OW0 WAT W 247 57.295 9.602 38.862 1.00 18.19 6459 OW0 WAT W 248 51.834 13.502 33.252 1.00 16.33 6460 OW0 WAT W 250 37.078 29.140 45.806 1.00 19.44 6461 OW0 WAT W 251 79.365 −4.623 6.311 1.00 27.30 6462 OW0 WAT W 252 50.994 3.684 58.665 1.00 26.14 6463 OW0 WAT W 253 16.237 1.326 45.058 1.00 21.57 6464 OW0 WAT W 254 59.347 18.360 43.822 1.00 21.00 6465 OW0 WAT W 255 93.718 −8.612 37.885 1.00 27.72 6466 OW0 WAT W 256 18.476 13.116 37.804 1.00 20.53 6467 OW0 WAT W 257 74.988 −1.264 7.841 1.00 23.15 6468 OW0 WAT W 258 65.708 −9.485 2.882 1.00 24.47 6469 OW0 WAT W 259 81.228 −18.556 15.613 1.00 21.70 6470 OW0 WAT W 260 40.153 18.506 50.014 1.00 29.11 6471 OW0 WAT W 261 76.275 −15.000 27.216 1.00 14.07 6472 OW0 WAT W 262 32.653 −11.672 30.238 1.00 24.10 6473 OW0 WAT W 263 33.719 19.637 32.612 1.00 23.35 6474 OW0 WAT W 264 57.975 6.308 29.825 1.00 28.17 6475 OW0 WAT W 265 56.014 3.037 13.415 1.00 27.45 6476 OW0 WAT W 266 35.289 −10.133 −21.987 1.00 24.36 6477 OW0 WAT W 267 48.772 −1.478 −18.710 1.00 22.08 6478 OW0 WAT W 268 56.907 −15.816 −21.447 1.00 21.69 6479 OW0 WAT W 269 70.103 −9.623 56.538 1.00 21.05 6480 OW0 WAT W 270 66.182 8.595 31.274 1.00 23.04 6481 OW0 WAT W 271 43.509 −7.089 −19.497 1.00 25.51 6482 OW0 WAT W 272 75.559 −23.596 13.036 1.00 25.28 6483 OW0 WAT W 273 52.581 11.622 50.505 1.00 19.81 6484 OW0 WAT W 274 70.407 −23.742 7.358 1.00 26.46 6485 OW0 WAT W 275 47.060 18.265 28.697 1.00 32.17 6486 OW0 WAT W 276 45.135 20.614 54.368 1.00 26.24 6487 OW0 WAT W 277 78.588 −20.221 12.456 1.00 28.74 6488 OW0 WAT W 278 26.272 −3.352 44.999 1.00 18.45 6489 OW0 WAT W 279 27.844 23.521 45.472 1.00 19.15 6490 OW0 WAT W 280 43.415 −9.483 −20.814 1.00 22.24 6491 OW0 WAT W 281 44.928 −9.823 21.085 1.00 21.62 6492 OW0 WAT W 282 67.718 4.640 5.963 1.00 25.19 6493 OW0 WAT W 283 96.982 −10.458 37.245 1.00 30.81 6494 OW0 WAT W 284 48.457 4.929 −7.033 1.00 23.97 6495 OW0 WAT W 285 55.985 −7.377 −3.129 1.00 27.03 6496 OW0 WAT W 286 35.786 −2.048 0.183 1.00 30.57 6497 OW0 WAT W 287 78.219 −5.390 40.921 1.00 16.49 6498 OW0 WAT W 288 77.364 −21.161 31.334 1.00 18.15 6499 OW0 WAT W 289 50.808 −19.872 31.259 1.00 23.98 6500 OW0 WAT W 290 31.863 −12.519 43.355 1.00 21.97 6501 OW0 WAT W 291 49.112 −1.399 15.411 1.00 32.14 6502 OW0 WAT W 292 36.747 2.739 53.684 1.00 28.77 6503 OW0 WAT W 293 47.932 −3.952 50.396 1.00 29.44 6504 OW0 WAT W 294 75.259 −18.091 42.038 1.00 27.99 6505 OW0 WAT W 295 65.026 17.315 32.530 1.00 25.64 6506 OW0 WAT W 296 78.244 −25.283 12.611 1.00 35.84 6507 OW0 WAT W 297 85.182 −4.003 27.099 1.00 38.09 6508 OW0 WAT W 298 58.707 −10.508 52.943 1.00 20.88 6509 OW0 WAT W 299 51.111 17.227 31.022 1.00 29.87 6510 OW0 WAT W 300 61.340 −13.950 17.572 1.00 27.41 6511 OW0 WAT W 301 38.209 −3.845 −22.771 1.00 26.19 6512 OW0 WAT W 302 72.914 −22.668 6.220 1.00 26.26 6513 OW0 WAT W 303 66.840 −21.476 4.405 1.00 27.43 6514 OW0 WAT W 304 50.616 −5.935 44.803 1.00 18.59 6515 OW0 WAT W 305 77.962 12.398 43.121 1.00 32.94 6516 OW0 WAT W 306 66.149 −13.682 −12.914 1.00 28.81 6517 OW0 WAT W 307 82.412 −2.518 2.943 1.00 26.24 6518 OW0 WAT W 308 37.840 23.041 26.322 1.00 28.62 6519 OW0 WAT W 309 61.723 −12.439 11.952 1.00 27.68 6520 OW0 WAT W 310 45.805 −15.302 29.600 1.00 42.22 6521 OW0 WAT W 311 37.738 11.900 54.333 1.00 30.73 6522 OW0 WAT W 312 78.463 −14.147 −10.311 1.00 23.91 6523 OW0 WAT W 313 46.583 −15.364 34.986 1.00 23.46 6524 OW0 WAT W 314 62.766 5.097 12.438 1.00 22.65 6525 OW0 WAT W 315 43.230 0.820 −21.984 1.00 35.81 6526 OW0 WAT W 316 43.950 4.358 −15.650 1.00 23.67 6527 OW0 WAT W 317 42.859 −10.546 45.639 1.00 32.28 6528 OW0 WAT W 318 49.162 −3.978 1.765 1.00 43.38 6529 OW0 WAT W 319 60.903 21.253 54.960 1.00 32.40 6530 OW0 WAT W 320 84.179 −7.984 18.419 1.00 21.93 6531 OW0 WAT W 321 44.701 −15.753 −5.792 1.00 24.15 6532 OW0 WAT W 322 17.649 6.695 35.037 1.00 33.00 6533 OW0 WAT W 323 39.424 −10.529 42.109 1.00 33.40 6534 OW0 WAT W 324 17.053 −3.033 44.924 1.00 32.20 6535 OW0 WAT W 325 71.659 −19.394 34.189 1.00 39.67 6536 OW0 WAT W 326 60.464 −11.885 54.688 1.00 29.00 6537 OW0 WAT W 327 60.150 8.501 29.954 1.00 22.12 6538 OW0 WAT W 328 71.908 12.459 33.945 1.00 31.00 6539 OW0 WAT W 329 50.518 −6.710 −4.970 1.00 24.35 6540 OW0 WAT W 330 81.378 −2.927 27.039 1.00 28.44 6541 OW0 WAT W 331 69.282 −16.298 45.601 1.00 27.45 6542 OW0 WAT W 332 67.427 −13.423 −6.333 1.00 30.02 6543 OW0 WAT W 333 46.329 −12.182 37.298 1.00 20.51 6544 OW0 WAT W 334 48.718 −20.006 −14.082 1.00 29.70 6545 OW0 WAT W 335 43.754 −13.207 36.811 1.00 26.82 6546 OW0 WAT W 336 64.098 14.236 26.166 1.00 29.05 6247 OW0 WAT W 337 37.049 3.266 −19.372 1.00 31.08 6548 OW0 WAT W 338 61.795 −10.158 −4.790 1.00 34.78 6549 OW0 WAT W 339 49.037 0.420 51.729 1.00 23.15 6550 OW0 WAT W 340 75.001 −18.929 4.449 1.00 25.65 6551 OW0 WAT W 341 65.358 −16.321 0.957 1.00 30.48 6552 OW0 WAT W 342 42.464 13.861 23.091 1.00 28.92 6553 OW0 WAT W 343 88.313 −2.838 44.183 1.00 29.50 6554 OW0 WAT W 344 32.606 12.506 24.842 1.00 22.59 6555 OW0 WAT W 345 56.691 16.693 46.428 1.00 23.81 6556 OW0 WAT W 346 91.741 −3.418 41.436 1.00 31.63 6557 OW0 WAT W 347 41.803 11.235 23.103 1.00 38.16 6558 OW0 WAT W 348 46.070 −13.919 32.782 1.00 29.90 6559 OW0 WAT W 349 54.505 −7.501 −20.473 1.00 30.31 6560 OW0 WAT W 350 80.666 −8.291 47.313 1.00 31.98 6561 OW0 WAT W 351 72.442 3.961 −1.194 1.00 29.66 6562 OW0 WAT W 352 37.415 6.655 27.782 1.00 26.05 6563 OW0 WAT W 353 68.123 −17.644 51.248 3.00 32.02 6564 OW0 WAT W 354 51.089 23.461 40.340 1.00 27.24 6565 OW0 WAT W 355 19.026 −6.909 51.121 1.00 26.68 6566 OW0 WAT W 356 34.952 4.204 −5.390 1.00 33.99 6567 OW0 WAT W 357 44.994 −11.459 33.261 1.00 25.35 6568 OW0 WAT W 358 45.207 −6.145 46.236 1.00 25.52 6569 OW0 WAT W 360 40.573 15.286 24.984 1.00 28.94 6570 OW0 WAT W 361 72.962 2.265 55.757 1.00 26.75 6571 OW0 WAT W 362 71.459 −26.046 4.160 1.00 28.61 6572 OW0 WAT W 363 38.402 20.036 48.661 1.00 22.55 6573 OW0 WAT W 364 32.615 21.884 33.926 1.00 31.74 6574 OW0 WAT W 365 80.451 −4.586 48.849 1.00 25.59 6575 OW0 WAT W 366 73.839 −20.204 6.685 1.00 23.97 6576 OW0 WAT W 367 79.652 −24.057 29.577 1.00 25.40 6577 OW0 WAT W 368 49.566 13.147 31.160 1.00 38.08 6578 OW0 WAT W 369 38.584 8.766 23.418 1.00 24.62 6579 OW0 WAT W 370 77.248 −23.896 30.696 1.00 25.85 6580 OW0 WAT W 371 77.989 −20.493 8.093 1.00 28.17 6581 OW0 WAT W 372 47.120 −18.023 33.871 1.00 30.24 6582 OW0 WAT W 373 10.465 5.660 47.993 1.00 36.55 6583 OW0 WAT W 374 57.307 14.254 27.302 1.00 27.17 6584 OW0 WAT W 375 38.985 13.275 24.929 1.00 23.57 6585 OW0 WAT W 376 72.047 −16.693 37.366 1.00 32.15 6586 OW0 WAT W 377 47.471 4.237 −17.052 1.00 36.00 6587 OW0 WAT W 378 51.129 −18.579 −13.092 1.00 23.58 6588 OW0 WAT W 379 86.696 −24.221 18.981 1.00 29.96 6589 OW0 WAT W 380 85.791 −0.516 37.710 1.00 29.15 6590 OW0 WAT W 381 84.814 −13.838 11.838 1.00 25.35 6591 OW0 WAT W 382 28.157 −11.801 44.088 1.00 22.15 6592 OW0 WAT W 383 62.926 22.843 35.656 1.00 35.59 6593 OW0 WAT W 384 17.572 0.721 42.711 1.00 18.81 6594 OW0 WAT W 385 75.014 −27.098 16.437 1.00 25.43 6595 OW0 WAT W 386 67.132 −16.141 −2.946 1.00 32.78 6596 OW0 WAT W 387 22.477 9.654 59.781 1.00 34.92 6597 OW0 WAT W 388 28.624 −2.581 27.502 1.00 40.90 6598 OW0 WAT W 389 68.480 5.583 25.870 1.00 20.19 6599 OW0 WAT W 390 72.335 −15.678 52.469 1.00 24.90 6600 OW0 WAT W 391 72.401 9.938 47.835 1.00 38.08 6601 OW0 WAT W 392 37.136 −4.896 3.579 1.00 39.22 6602 OW0 WAT W 393 87.130 −3.587 22.928 1.00 28.96 6603 OW0 WAT W 394 59.733 21.534 42.236 1.00 19.04 6604 OW0 WAT W 395 49.614 −6.092 47.633 1.00 26.38 6605 OW0 WAT W 396 68.508 −18.979 0.775 1.00 25.22 6606 OW0 WAT W 397 30.344 16.345 53.767 1.00 21.53 6607 OW0 WAT W 398 36.689 −10.063 44.341 1.00 27.75 6608 OW0 WAT W 399 44.255 10.317 20.950 1.00 38.55 6609 OW0 WAT W 400 80.351 −27.377 31.973 1.00 29.96 6610 OW0 WAT W 401 62.323 −7.884 −10.201 1.00 25.19 6611 OW0 WAT W 402 48.124 −18.230 −10.307 1.00 28.48 6612 OW0 WAT W 403 61.453 −14.796 −18.703 1.00 40.45 6613 OW0 WAT W 404 66.241 −21.530 28.934 1.00 30.44 6614 OW0 WAT W 405 39.152 22.713 47.906 1.00 17.90 6615 OW0 WAT W 406 46.042 −16.832 −9.093 1.00 35.13 6616 OW0 WAT W 407 63.039 0.557 60.763 1.00 33.78 6617 OW0 WAT W 408 64.512 10.494 17.998 1.00 31.21 6618 OW0 WAT W 409 66.376 −17.542 55.784 1.00 21.41 6619 OW0 WAT W 410 47.053 −15.752 −6.786 1.00 27.55 6620 OW0 WAT W 411 25.339 −10.076 43.114 1.00 23.49 6621 OW0 WAT W 412 66.204 −5.949 25.409 1.00 30.80 6622 OW0 WAT W 413 38.412 −12.030 33.503 1.00 27.23 6623 OW0 WAT W 414 33.850 28.896 42.331 1.00 47.21 6624 OW0 WAT W 415 17.795 16.340 37.828 1.00 33.59 6625 OW0 WAT W 416 34.565 −12.132 −23.818 1.00 31.86 6626 OW0 WAT W 417 91.832 −14.160 17.359 1.00 37.03 6627 OW0 WAT W 418 47.439 14.844 32.551 1.00 33.39 6628 OW0 WAT W 419 69.434 −25.542 21.203 1.00 41.60 6629 OW0 WAT W 420 55.830 −14.109 41.979 1.00 51.22 6630 OW0 WAT W 421 42.926 −12.881 34.347 1.00 23.83 6631 OW0 WAT W 422 63.743 −0.676 4.790 1.00 36.35 6632 OW0 WAT W 423 55.526 0.391 11.719 1.00 43.19 6633 OW0 WAT W 424 73.417 12.097 49.004 1.00 38.46 6634 OW0 WAT W 425 52.369 24.730 35.218 1.00 28.92 6635 OW0 WAT W 426 62.668 −12.567 −11.718 1.00 28.63 6636 OW0 WAT W 427 64.528 −14.519 −11.603 1.00 34.77 6637 OW0 WAT W 428 85.369 −26.700 28.869 1.00 34.96 6638 OW0 WAT W 429 34.890 11.971 56.023 1.00 30.32 6639 OW0 WAT W 430 38.319 13.761 52.914 1.00 38.81 6640 OW0 WAT W 431 36.205 −3.725 22.946 1.00 38.51 6641 OW0 WAT W 432 61.755 −18.698 19.722 1.00 32.41 6642 OW0 WAT W 433 73.740 −17.674 33.635 1.00 36.99 6643 OW0 WAT W 434 62.176 −18.812 26.590 1.00 35.56 6644 OW0 WAT W 435 80.166 −4.065 15.814 1.00 41.24 6645 OW0 WAT W 436 63.537 −3.108 10.225 1.00 26.01 6646 OW0 WAT W 437 70.855 11.063 55.846 1.00 38.80 6647 OW0 WAT W 438 55.025 19.284 36.156 1.00 21.38 6648 OW0 WAT W 439 82.953 −0.517 19.836 1.00 31.57 6649 OW0 WAT W 440 77.688 3.005 35.260 1.00 27.61 6650 OW0 WAT W 441 47.174 −19.776 −25.723 1.00 25.70 6651 OW0 WAT W 442 15.282 −0.724 48.333 1.00 63.95 6652 OW0 WAT W 443 45.668 2.364 56.289 1.00 29.20 6653 OW0 WAT W 444 55.704 7.505 11.701 1.00 31.83 6654 OW0 WAT W 445 41.558 6.741 55.087 1.00 34.44 6655 OW0 WAT W 446 73.701 7.136 28.230 1.00 26.54 6656 OW0 WAT W 447 21.624 11.628 31.608 1.00 30.60 6657 OW0 WAT W 448 97.126 −16.727 30.310 1.00 34.64 6658 OW0 WAT W 449 74.340 −4.743 24.963 1.00 45.37 6659 OW0 WAT W 450 84.402 −6.566 16.139 1.00 30.72 6660 OW0 WAT W 451 28.262 21.244 24.604 1.00 43.08 6661 OW0 WAT W 452 23.084 1.809 31.647 1.00 26.48 6662 OW0 WAT W 453 42.394 −4.193 3.333 1.00 31.81 6663 OW0 WAT W 454 62.371 −1.473 8.394 1.00 27.83 6664 OW0 WAT W 455 46.837 6.251 21.345 1.00 36.13 6665 OW0 WAT W 456 35.480 26.992 45.795 1.00 28.88 6666 OW0 WAT W 457 51.976 −7.138 −1.858 1.00 31.75 6667 OW0 WAT W 458 69.604 −18.226 42.817 1.00 31.57 6668 OW0 WAT W 459 68.233 −16.493 −13.125 1.90 34.37 6669 OW0 WAT W 460 38.919 4.604 −15.945 1.00 30.77 6670 OW0 WAT W 461 54.603 −1.784 −10.268 1.00 29.83 6671 OW0 WAT W 462 75.522 −18.796 38.966 1.00 35.67 6672 OW0 WAT W 463 81.655 −2.401 17.151 1.00 32.07 6673 OW0 WAT W 464 57.826 −19.166 25.096 1.00 38.97 6674 OW0 WAT W 465 81.263 −20.540 14.119 1.00 33.94 6675 OW0 WAT W 466 63.386 −6.403 6.370 1.00 39.46 6676 OW0 WAT W 467 81.257 0.044 −1.327 1.00 37.79 6677 OW0 WAT W 468 46.062 −15.455 −25.516 1.00 41.40 6678 OW0 WAT W 469 20.247 20.109 38.622 1.00 27.65 6679 OW0 WAT W 470 77.490 −21.509 14.231 1.00 36.26 6680 OW0 WAT W 471 76.196 −24.636 0.276 1.00 43.65 6681 OW0 WAT W 472 30.399 24.885 35.289 1.00 33.93 6682 OW0 WAT W 473 30.055 13.347 25.308 1.00 32.70 6683 OW0 WAT W 474 84.910 −4.142 0.423 1.00 39.08 6684 OW0 WAT W 475 31.259 0.007 −12.949 1.00 31.64 6685 OW0 WAT W 476 36.835 26.993 49.651 1.00 27.17 6686 OW0 WAT W 477 90.488 −25.441 33.765 1.00 38.84 6687 OW0 WAT W 478 58.971 15.316 62.875 1.00 38.57 6688 OW0 WAT W 479 71.338 −25.348 1.040 1.00 55.72 6689 OW0 WAT W 480 43.705 −19.415 −13.619 1.00 37.68 6690 OW0 WAT W 481 69.730 14.867 50.512 1.00 26.27 6691 OW0 WAT W 482 14.828 13.346 51.319 1.00 27.62 6692 OW0 WAT W 483 90.856 −21.318 −3.133 1.00 53.86 6693 OW0 WAT W 484 56.183 −9.627 16.617 1.00 30.41 6694 OW0 WAT W 485 57.382 −1.553 −6.767 1.00 29.36 6695 OW0 WAT W 486 37.727 −6.554 −23.027 1.00 31.09 6696 OW0 WAT W 487 60.051 24.897 33.921 1.00 48.03 6697 OW0 WAT W 488 17.634 15.818 50.213 1.00 46.53 6698 OW0 WAT W 489 78.778 −24.898 44.836 1.00 40.33 6699 OW0 WAT W 490 65.719 9.772 60.623 1.00 47.51 6700 OW0 WAT W 491 21.58.3 −9.599 41.401 1.00 37.21 6701 OW0 WAT W 492 47.040 2.603 20.841 1.00 34.24 6702 OW0 WAT W 493 54.279 1.535 −18.697 1.00 44.41 6703 OW0 WAT W 494 62.066 −1.934 −8.477 1.00 39.01 6704 OW0 WAT W 495 30.722 −7.382 −7.418 1.00 34.70 6705 OW0 WAT W 496 31.310 1.784 −6.926 1.09 31.46 6706 OW0 WAT W 497 52.330 11.012 30.962 1.00 32.49 6707 OW0 WAT W 498 65.945 −20.083 21.418 1.00 30.34 6708 OW0 WAT W 499 50.770 −10.173 12.866 1.00 47.95 6709 OW0 WAT W 500 61.046 23.935 37.360 1.00 32.34 6710 OW0 WAT W 501 39.600 2.991 −0.996 1.00 46.45 6711 OW0 WAT W 502 27.724 −11.311 40.533 1.00 16.56 6712 OW0 WAT W 503 59.536 −2.849 −8.699 1.00 28.34 6713 OW0 WAT W 504 40.735 24.000 49.923 1.00 34.03 6714 OW0 WAT W 505 73.997 −27.214 14.115 1.00 43.47 6715 OW0 WAT W 506 40.887 −10.965 33.589 1.00 26.99 6716 OW0 WAT W 507 82.531 3.559 45.765 1.00 30.67 6717 OW0 WAT W 508 48.547 −17.731 −5.638 1.00 44.65 6718 OW0 WAT W 509 40.883 −5.002 48.490 1.00 31.16 6719 OW0 WAT W 510 76.430 −25.387 32.925 1.00 30.36 6720 OW0 WAT W 511 71.990 12.764 51.191 1.00 30.30 6721 OW0 WAT W 512 20.681 0.962 54.358 1.00 33.83 6722 OW0 WAT W 513 27.139 25.062 36.224 1.00 39.95 6723 OW0 WAT W 514 83.997 −20.448 13.120 1.00 46.83 6724 OW0 WAT W 515 79.230 −24.653 37.743 1.00 35.45 6725 OW0 WAT W 516 38.032 −10.688 −25.566 1.00 31.11 6726 OW0 WAT W 517 88.040 −1.843 36.126 1.00 30.26 6727 OW0 WAT W 518 71.250 15.795 48.528 1.00 29.38 6728 OW0 WAT W 520 15.848 7.343 57.167 1.00 32.22 6729 OW0 WAT W 521 34.398 −21.215 −9.737 1.00 44.50 6730 OW0 WAT W 522 64.038 −6.164 54.619 1.00 32.76 6731 OW0 WAT W 523 64.354 1.072 −3.179 1.00 29.78 6732 OW0 WAT W 524 85.120 3.839 36.045 1.00 40.08 6733 OW0 WAT W 525 86.257 2.953 41.138 1.00 41.59 6734 OW0 WAT W 526 52.892 6.449 29.807 1.00 29.56 6735 OW0 WAT W 527 44.099 5.976 −11.549 1.00 27.68 6736 OW0 WAT W 528 54.883 −0.564 −7.820 1.00 28.79 6737 OW0 WAT W 529 80.659 −25.958 36.000 1.00 43.82 6738 OW0 WAT W 530 77.061 −1.218 13.093 1.00 33.25 6739 OW0 WAT W 531 12.960 2.681 41.428 1.00 40.30 6740 OW0 WAT W 532 15.085 14.951 49.204 1.00 33.19 6741 OW0 WAT W 533 66.186 −17.851 36.224 1.00 44.47 6742 OW0 WAT W 534 33.556 −7.708 −22.528 1.00 36.36 6743 OW0 WAT W 535 64.789 −11.150 5.378 1.00 30.63 6744 OW0 WAT W 536 60.271 6.086 27.464 1.00 32.06 6745 OW0 WAT W 537 90.487 −15.669 14.264 1.00 35.70 6746 OW0 WAT W 538 79.423 −0.659 26.417 1.00 32.82 6747 OW0 WAT W 539 27.499 −9.225 41.241 1.00 38.84 6748 OW0 WAT W 540 38.460 −17.144 −22.854 1.00 32.97 6749 OW0 WAT W 541 95.109 −18.447 21.117 1.00 45.20 6750 OW0 WAT W 542 46.885 1.862 −21.845 1.00 45.25 6751 OW0 WAT W 543 72.300 15.489 37.082 1.00 38.81 6752 OW0 WAT W 544 53.484 −19.303 24.437 1.00 31.94 6753 OW0 WAT W 545 68.271 −16.075 53.457 1.00 33.31 6754 OW0 WAT W 546 81.187 −12.562 8.492 1.00 31.48 6755 OW0 WAT W 547 49.103 −15.891 43.116 1.00 33.62 6756 OW0 WAT W 548 63.252 −20.824 18.880 1.00 38.97 6757 OW0 WAT W 549 86.032 −2.093 25.031 1.00 38.83 6758 OW0 WAT W 550 50.812 −9.392 −2.366 1.00 32.70 6759 OW0 WAT W 551 77.222 −22.310 5.262 1.00 42.02 6760 OW0 WAT W 552 87.105 0.417 40.246 1.00 33.75 6761 OW0 WAT W 553 39.779 −10.913 28.103 1.00 32.23 6762 OW0 WAT W 554 80.530 5.700 44.684 1.00 22.37 6763 OW0 WAT W 555 44.445 21.933 51.741 1.00 40.68 6764 OW0 WAT W 556 78.037 4.895 33.580 1.00 38.94 6765 OW0 WAT W 557 50.788 −1.091 53.731 1.00 40.29 6766 OW0 WAT W 558 48.427 −18.608 31.494 1.00 38.93 6767 OW0 WAT W 559 36.861 8.729 55.912 1.00 32.41 6768 OW0 WAT W 560 34.764 8.292 57.897 1.00 41.50 6769 OW0 WAT W 561 52.719 −18.428 −15.193 1.00 34.83 6770 OW0 WAT W 562 21.141 21.506 43.413 1.00 35.68 6771 OW0 WAT W 563 32.675 10.931 22.641 1.00 33.70 6772 OW0 WAT W 564 79.498 −28.457 28.133 1.00 41.72 6773 OW0 WAT W 565 31.047 −13.425 34.555 1.00 32.76 6774 OW0 WAT W 566 17.333 −4.663 51.771 1.00 23.15 6775 OW0 WAT W 567 73.981 −25.793 −1.995 1.00 46.66 6776 OW0 WAT W 568 54.933 7.887 31.452 1.00 35.09 6777 OW0 WAT W 569 40.812 −13.172 37.899 1.00 34.36 6778 OW0 WAT W 570 90.118 −22.677 43.385 1.00 42.30 6779 OW0 WAT W 571 49.795 16.333 32.935 1.00 33.34 6780 OW0 WAT W 572 86.224 −3.103 29.568 1.00 45.18 6781 OW0 WAT W 573 93.985 −21.583 25.927 1.00 49.38 6782 OW0 WAT W 574 48.711 29.216 31.209 1.00 38.64 6783 OW0 WAT W 575 80.779 −26.481 29.557 1.00 41.33 6784 OW0 WAT W 576 30.291 −0.331 −3.469 1.00 33.78 6785 OW0 WAT W 577 83.004 −7.012 12.342 1.00 54.12 6786 OW0 WAT W 578 77.402 10.589 36.940 1.00 34.01 6787 OW0 WAT W 579 36.261 17.002 46.660 1.00 36.83 6788 OW0 WAT W 580 72.862 13.977 47.223 1.00 31.19 6789 OW0 WAT W 581 47.939 −15.855 24.111 1.00 32.81 6790 OW0 WAT W 582 77.692 6.100 24.255 1.00 39.63 6791 OW0 WAT W 583 64.653 −13.766 4.879 1.00 38.84 6792 OW0 WAT W 584 46.486 −2.333 51.867 1.00 65.57 6793 OW0 WAT W 585 76.557 6.773 47.617 1.00 30.60 6794 OW0 WAT W 586 55.689 0.519 60.810 1.00 37.55 6795 OW0 WAT W 587 77.597 −7.073 50.855 1.00 34.75 6796 OW0 WAT W 588 88.395 −13.032 11.580 1.00 29.59 6797 OW0 WAT W 589 41.920 18.111 24.362 1.00 32.25 6798 OW0 WAT W 590 37.249 −12.482 31.297 1.00 28.69 6799 OW0 WAT W 591 82.022 −21.727 0.851 1.00 41.41 6800 OW0 WAT W 592 74.315 9.720 29.056 1.00 36.96 6801 OW0 WAT W 593 51.410 5.026 −6.751 1.00 40.52 6802 OW0 WAT W 594 47.526 10.717 59.474 1.00 44.35 6803 OW0 WAT W 595 53.540 −15.820 20.692 1.00 36.01 6804 OW0 WAT W 596 34.459 −9.657 26.624 1.00 33.62 6805 OW0 WAT W 597 67.159 18.723 29.650 1.00 47.65 6806 OW0 WAT W 598 57.902 −6.416 11.043 1.00 36.87 6807 OW0 WAT W 599 33.150 10.072 56.599 1.00 36.61 6808 OW0 WAT W 600 80.247 −13.720 45.923 1.00 38.71 6809 OW0 WAT W 601 65.256 5.486 60.044 1.00 25.49 6810 OW0 WAT W 602 70.764 −21.357 −4.897 1.00 34.79 6811 OW0 WAT W 603 43.485 −13.298 22.439 1.00 36.93 6812 OW0 WAT W 604 55.370 23.838 31.451 1.00 40.61 6813 OW0 WAT W 605 72.230 −4.477 53.756 1.00 33.63 6814 OW0 WAT W 606 86.015 −6.308 44.482 1.00 33.31 6815 OW0 WAT W 607 79.100 6.742 28.261 1.00 36.39 6816 OW0 WAT W 608 13.024 10.093 41.592 1.00 39.66 6817 OW0 WAT W 610 19.065 2.738 56.666 1.00 36.22 6818 OW0 WAT W 611 27.658 18.474 28.229 1.00 29.78 6819 OW0 WAT W 612 79.524 −22.097 −5.261 1.00 35.00 6820 OW0 WAT W 613 78.777 3.843 −0.369 1.00 39.60 6821 OW0 WAT W 614 60.674 23.492 32.021 1.00 50.31 6822 OW0 WAT W 615 89.369 −13.520 6.901 1.00 53.93 6823 OW0 WAT W 616 54.674 2.066 −7.514 1.00 35.44 6824 OW0 WAT W 617 80.241 −21.114 10.183 1.00 45.60 6825 OW0 WAT W 618 39.869 −0.368 53.204 1.00 31.86 6826 OW0 WAT W 619 84.314 0.222 22.029 1.00 38.74 6827 OW0 WAT W 620 77.764 −28.451 25.257 1.00 42.43 6828 OW0 WAT W 621 92.860 −6.918 29.400 1.00 43.50 6829 OW0 WAT W 623 82.066 −22.011 −5.845 1.00 43.27 6830 OW0 WAT W 624 66.952 21.443 36.324 1.00 35.06 6831 OW0 WAT W 625 65.091 −21.080 25.542 1.00 36.11 6832 OW0 WAT W 626 95.260 −15.509 41.378 1.00 32.64 6833 OW0 WAT W 627 60.917 −1.177 −13.410 1.00 40.04 6834 OW0 WAT W 628 60.376 −14.353 56.761 1.00 47.88 6835 OW0 WAT W 629 35.528 −17.752 −20.354 1.00 38.18 6836 OW0 WAT W 630 53.084 17.303 25.669 1.00 46.68 6837 OW0 WAT W 631 49.338 24.584 23.434 1.00 37.08 6838 OW0 WAT W 632 44.633 31.369 41.827 1.00 51.68 6839 OW0 WAT W 633 41.364 9.274 55.363 1.00 48.19 6840 OW0 WAT W 634 85.480 −8.670 45.623 1.00 38.50 6841 OW0 WAT W 635 67.366 8.090 27.660 1.00 46.28 6842 OW0 WAT W 636 58.044 20.208 61.858 1.00 43.81 6843 OW0 WAT W 637 60.247 −6.665 −19.077 1.00 33.84 6844 OW0 WAT W 638 22.729 2.441 55.615 1.00 38.38 6845 OW0 WAT W 639 58.636 −8.488 −2.049 1.00 45.41 6846 OW0 WAT W 640 51.765 −5.454 −24.427 1.00 30.07 6847 OW0 WAT W 641 60.477 −7.078 −5.334 1.00 51.94 6848 OW0 WAT W 642 35.217 24.951 48.021 1.00 36.69 6849 OW0 WAT W 643 25.477 8.964 26.926 1.00 36.50 6850 OW0 WAT W 644 73.038 7.145 25.686 1.00 38.10 6851 OW0 WAT W 645 31.546 26.839 42.458 1.00 37.72 6852 OW0 WAT W 646 78.629 5.276 46.680 1.00 31.14 6853 OW0 WAT W 647 50.352 −10.415 0.030 1.00 34.69 6854 OW0 WAT W 648 23.075 3.622 57.785 1.00 50.55 6855 OW0 WAT W 649 82.155 −23.495 3.245 1.00 34.51 6856 OW0 WAT W 650 53.614 −0.820 −5.533 1.00 30.46 6857 OW0 WAT W 651 41.173 6.120 −12.244 1.00 32.87 6858 OW0 WAT W 652 46.461 15.785 29.821 1.00 33.74 6859 OW0 WAT W 653 46.910 −0.266 53.614 1.00 36.78 6860 OW0 WAT W 654 54.969 9.457 27.413 1.00 41.28 6861 OW0 WAT W 655 71.413 4.824 11.859 1.00 47.81 6862 OW0 WAT W 656 48.713 3.240 −19.259 1.00 36.50 6863 OW0 WAT W 657 53.539 25.302 32.981 1.00 38.05 6864 OW0 WAT W 658 53.590 −1.475 8.457 1.00 51.45 6865 OW0 WAT W 659 79.662 −22.479 −0.183 1.00 50.01 6866 OW0 WAT W 660 18.141 15.650 34.789 1.00 53.01 6867 OW0 WAT W 661 87.154 −0.180 42.783 1.00 47.33 6868 OW0 WAT W 662 62.459 9.375 29.050 1.00 30.93 6869 OW0 WAT W 663 42.984 25.814 49.065 1.00 34.72 6870 OW0 WAT W 664 89.832 −5.536 43.041 1.00 35.89 6871 OW0 WAT W 666 95.356 −6.463 30.956 1.00 39.83 6872 OW0 WAT W 667 70.567 14.899 27.721 1.00 47.74 6873 OW0 WAT W 668 38.060 1.861 56.019 1.00 43.81 6874 OW0 WAT W 669 42.573 −12.553 29.782 1.00 44.56 6875 OW0 WAT W 670 63.052 −18.013 29.178 1.00 32.11 6876 OW0 WAT W 671 26.904 −12.528 −19.449 1.00 50.32 6877 OW0 WAT W 672 87.381 −14.602 9.308 1.00 38.68 6878 OW0 WAT W 673 73.626 −6.763 27.221 1.00 44.79 6879 OW0 WAT W 674 19.297 10.427 29.648 1.00 53.79 6880 OW0 WAT W 675 61.974 −17.776 43.690 1.00 45.64 6881 OW0 WAT W 676 21.734 16.509 28.603 1.00 52.65 6882 OW0 WAT W 677 90.154 −12.035 4.840 1.00 52.27 6883 OW0 WAT W 678 77.008 5.083 18.362 1.00 38.43 6884 OW0 WAT W 679 78.849 −3.340 8.660 1.00 44.26 6885 OW0 WAT W 680 37.125 6.546 25.017 1.00 26.76 6886 OW0 WAT W 681 65.476 13.560 57.511 1.00 38.57 6887 OW0 WAT W 682 54.416 3.948 15.578 1.00 40.81 6888 OW0 WAT W 683 53.062 −18.088 22.008 1.00 43.19 6889 OW0 WAT W 684 12.292 12.538 42.132 1.00 32.07 6890 OW0 WAT W 685 22.880 9.102 31.205 1.00 44.59 6891 OW0 WAT W 686 24.576 −0.920 55.112 1.00 42.14 6892 OW0 WAT W 687 61.965 −4.738 11.865 1.00 34.12 6893 OW0 WAT W 688 54.878 −16.136 18.394 1.00 42.78 6894 OW0 WAT W 689 16.847 19.568 45.126 1.00 43.60 6895 OW0 WAT W 690 55.170 23.039 52.155 1.00 41.75 6896 OW0 WAT W 691 39.834 −12.044 −3.476 1.00 36.25 6897 OW0 WAT W 692 83.900 −19.454 48.185 1.00 42.85 6898 OW0 WAT W 693 62.276 19.955 30.431 1.00 34.17 6899 OW0 WAT W 694 84.970 −6.738 10.835 1.00 42.23 6900 OW0 WAT W 695 35.725 −14.462 31.165 1.00 39.86 6901 OW0 WAT W 696 58.055 17.975 63.613 1.00 53.19 6902 OW0 WAT W 697 48.858 27.436 43.339 1.00 47.28 6903 OW0 WAT W 698 63.336 −8.234 57.236 1.00 47.00 6904 OW0 WAT W 699 70.147 −26.087 29.342 1.00 55.27 6905 OW0 WAT W 700 66.692 −14.096 −16.368 1.00 45.91 6906 OW0 WAT W 701 40.692 15.224 56.764 1.00 46.42 6907 OW0 WAT W 702 79.719 −28.791 22.760 1.00 32.02 6908 OW0 WAT W 703 59.465 21.759 30.551 1.00 42.42 6909 OW0 WAT W 704 31.141 −5.131 22.552 1.00 68.52 6910 OW0 WAT W 705 36.695 −16.973 −4.878 1.00 37.89 6911 OW0 WAT W 706 80.687 −20.765 47.298 1.00 38.30 6912 OW0 WAT W 707 54.669 3.010 −9.815 1.00 46.05 6913 OW0 WAT W 708 43.216 −8.260 47.123 1.00 40.03 6914 OW0 WAT W 709 70.862 15.600 41.973 1.00 37.00 6915 OW0 WAT W 710 33.412 −2.522 54.114 1.00 48.11 6916 OW0 WAT W 711 92.535 −0.923 34.738 1.00 49.47 6917 OW0 WAT W 712 33.025 23.917 47.317 1.00 46.24 6918 OW0 WAT W 713 70.249 17.850 37.204 1.00 40.78 6919 OW0 WAT W 714 41.368 22.495 53.675 1.00 40.32 6920 OW0 WAT W 715 76.578 −19.899 49.657 1.00 40.87 6921 OW0 WAT W 716 90.425 −4.420 30.203 1.00 60.30 6922 OW0 WAT W 717 34.487 19.062 20.833 1.00 45.89 6923 OW0 WAT W 718 89.801 −4.016 22.869 1.00 46.61 6924 OW0 WAT W 719 74.377 1.047 −13.486 1.00 51.80 6925 OW0 WAT W 720 66.403 4.257 9.718 1.00 41.97 6926 OW0 WAT W 721 56.444 −17.979 −12.402 1.00 40.83 6927 OW0 WAT W 722 82.588 −0.182 1.654 1.00 55.22 6928 OW0 WAT W 723 61.949 −0.825 −0.993 1.00 44.85 6929 OW0 WAT W 724 94.665 −3.882 41.279 1.00 43.45 6930 OW0 WAT W 725 78.637 −22.418 46.944 1.00 49.42 6931 OW0 WAT W 726 76.801 0.776 11.150 1.00 43.15 6932 OW0 WAT W 727 36.682 26.179 34.703 1.00 46.16 6933 OW0 WAT W 728 52.946 −24.152 35.886 1.00 42.32 6934 OW0 WAT W 729 44.065 −10.820 0.741 1.00 58.49 6935 OW0 WAT W 730 59.442 −15.880 42.690 1.00 31.69 6936 OW0 WAT W 731 72.384 8.537 51.566 1.00 31.82 6937 OW0 WAT W 732 31.347 −6.053 26.265 1.00 42.64 6938 OW0 WAT W 733 34.630 6.679 23.929 1.00 43.41 6939 OW0 WAT W 734 57.088 −11.759 −15.829 1.00 40.44 6940 OW0 WAT W 735 79.179 −22.870 6.833 1.00 45.12 6941 OW0 WAT W 736 38.310 −14.037 35.139 1.00 44.86 6942 OW0 WAT W 737 39.171 −2.907 53.911 1.00 45.60 6943 OW0 WAT W 738 39.322 17.940 52.385 1.00 42.20 6944 OW0 WAT W 739 48.359 2.635 58.769 1.00 51.66 6945 OW0 WAT W 740 72.823 5.269 52.825 1.00 45.87 6946 OW0 WAT W 741 52.762 19.727 28.434 1.00 40.22 6947 OW0 WAT W 742 28.202 −5.793 −6.513 1.00 48.77 6948 OW0 WAT W 743 79.618 1.235 4.432 1.00 42.94 6949 OW0 WAT W 744 67.094 −18.257 47.501 1.00 38.02 6950 OW0 WAT W 745 52.688 10.357 62.956 1.00 40.29 6951 OW0 WAT W 746 40.431 −14.509 −4.481 1.00 42.77 6952 OW0 WAT W 747 38.750 −10.992 22.885 1.00 44.88 6953 OW0 WAT W 748 44.292 14.402 59.454 1.00 44.70 6954 OW0 WAT W 749 88.953 −23.063 20.219 1.00 41.34 6955 OW0 WAT W 750 56.654 −11.968 83.046 1.00 60.38 6956 OW0 WAT W 751 41.969 29.748 47.846 1.00 20.80 6957 OW0 WAT W 752 44.966 −16.181 23.899 1.00 50.48 6958 OW0 WAT W 753 85.644 −22.932 2.568 1.00 43.55 6959 OW0 WAT W 754 43.034 6.314 −21.514 1.00 51.86 6960 OW0 WAT W 755 84.872 4.181 42.842 1.00 49.44 6961 OW0 WAT W 756 74.363 11.696 34.959 1.00 37.97 6962 OW0 WAT W 757 80.803 5.977 33.052 1.00 43.23 6963 OW0 WAT W 758 61.280 17.301 88.888 1.00 40.96 6964 OW0 WAT W 759 35.859 19.793 23.282 1.00 48.10 6965 OW0 WAT W 760 20.148 19.237 32.614 1.00 31.76 6966 OW0 WAT W 761 15.289 11.762 36.214 1.00 43.45 6967 OW0 WAT W 762 46.595 −5.917 −22.133 1.00 44.31 6968 OW0 WAT W 763 20.413 11.283 60.057 1.00 50.11 6969 OW0 WAT W 764 68.167 5.712 13.653 1.00 30.67 6970 OW0 WAT W 765 54.184 2.615 −12.252 1.00 39.38 6971 OW0 WAT W 766 84.664 −22.555 14.359 1.00 45.78 6972 OW0 WAT W 767 30.072 −20.212 −10.959 1.00 38.35 6973 OW0 WAT W 768 41.072 −0.946 −21.837 1.00 41.66 6974 OW0 WAT W 769 61.874 11.916 27.798 1.00 44.81 6975 OW0 WAT W 770 66.356 5.178 −1.773 1.00 65.15 6976 OW0 WAT W 771 26.844 5.186 59.968 1.00 46.27 6977 OW0 WAT W 772 36.878 24.305 28.318 1.00 34.70 6978 OW0 WAT W 773 54.912 −1.550 −21.819 1.00 42.64 6979 OW0 WAT W 774 59.594 −17.858 41.366 1.00 37.27 6980 OW0 WAT W 775 57.520 −15.150 18.294 1.00 36.30 6981 OW0 WAT W 776 32.998 24.523 34.342 1.00 42.23 6982 OW0 WAT W 777 59.020 −12.114 56.789 1.00 57.61 6983 OW0 WAT W 778 81.113 −27.278 43.621 1.00 41.79 6984 OW0 WAT W 779 73.319 −20.756 38.654 1.00 43.17 6985 OW0 WAT W 780 78.478 −16.566 37.845 1.00 51.42 6986 OW0 WAT W 781 91.610 −6.042 15.770 1.00 36.38 6987 OW0 WAT W 782 71.605 16.644 39.410 1.00 48.62 6988 OW0 WAT W 783 63.508 24.207 41.029 1.00 44.22 6989 OW0 WAT W 784 88.822 −11.109 7.822 1.00 48.78 6990 OW0 WAT W 785 71.691 −23.906 33.801 1.00 48.29 6991 OW0 WAT W 786 52.032 8.913 29.301 1.00 39.41 6992 OW0 WAT W 787 72.141 14.023 31.846 1.00 37.55 6993 OW0 WAT W 788 39.138 16.149 26.862 1.00 50.27 6994 OW0 WAT W 789 37.813 −9.039 47.875 1.00 13.18 6995 OW0 WAT W 790 35.173 −8.363 50.198 1.00 39.87 6996 OW0 WAT W 791 26.847 −1.258 31.548 1.00 39.21 6997 OW0 WAT W 792 88.614 −23.766 1.624 1.00 54.25 6998 OW0 WAT W 793 21.121 7.089 31.169 1.00 50.12 6999 OW0 WAT W 794 41.636 21.622 50.969 1.00 47.76 7000 OW0 WAT W 795 26.421 0.362 29.613 1.00 43.60 7001 OW0 WAT W 796 44.401 −8.843 −23.747 1.00 40.62 7002 OW0 WAT W 797 70.057 18.053 42.138 1.00 38.85 7003 OW0 WAT W 798 66.270 −17.604 −6.916 1.00 45.58 7004 OW0 WAT W 799 46.164 31.367 45.417 1.00 51.35 7005 OW0 WAT W 800 78.137 5.508 51.679 1.00 45.47 7006 OW0 WAT W 801 18.046 3.941 59.147 1.00 42.23 7007 OW0 WAT W 802 89.339 0.402 −2.076 1.00 52.88 7008 OW0 WAT W 803 55.564 −18.287 −15.179 1.00 38.85 7009 OW0 WAT W 804 28.418 0.009 26.267 1.00 52.59 7010 OW0 WAT W 805 97.132 −12.269 27.826 1.00 38.21 7011 OW0 WAT W 806 21.485 21.769 33.106 1.00 37.99 7012 OW0 WAT W 807 61.494 −16.277 −11.458 1.00 32.24 7013 OW0 WAT W 808 77.944 −0.349 8.828 1.00 56.65 7014 OW0 WAT W 809 75.983 −17.170 −12.760 1.00 35.83 7015 OW0 WAT W 810 52.665 −11.955 −2.121 1.00 42.38 7016 OW0 WAT W 811 54.291 −1.443 −1.785 1.00 38.65 7017 OW0 WAT W 812 51.272 6.345 31.812 1.00 46.84 7018 OW0 WAT W 813 96.248 −8.528 40.673 1.00 36.47 7019 OW0 WAT W 814 21.883 −7.783 54.051 1.00 37.11 7020 OW0 WAT W 815 41.687 30.174 33.806 1.00 43.95 7021 OW0 WAT W 816 49.364 −19.438 −8.102 1.00 46.98 7022 OW0 WAT W 817 63.992 20.309 53.102 1.00 38.77 7023 OW0 WAT W 818 65.323 12.002 26.726 1.00 45.31 7024 OW0 WAT W 819 44.245 −15.998 36.333 1.00 36.72 7025 OW0 WAT W 820 61.512 −12.703 −20.772 1.00 42.86 7026 OW0 WAT W 821 40.874 −3.535 −22.568 1.00 37.17 7027 OW0 WAT W 822 53.950 22.361 28.394 1.00 48.45 7028 OW0 WAT W 823 47.488 6.176 −13.884 1.00 39.21 7029 OW0 WAT W 824 62.078 −1.860 61.143 1.00 48.06 7030 OW0 WAT W 825 83.442 −26.335 2.633 1.00 59.67 7031 OW0 WAT W 826 82.792 −0.371 24.014 1.00 41.82 7032 OW0 WAT W 827 49.612 12.353 60.988 1.00 43.87 7033 OW0 WAT W 828 41.022 −7.720 48.703 1.00 39.62 7034 OW0 WAT W 829 64.480 1.533 −6.989 1.00 39.53 7035 OW0 WAT W 830 19.350 12.831 57.326 1.00 35.73 7036 OW0 WAT W 831 22.229 14.191 30.825 1.00 54.08 7037 OW0 WAT W 832 69.924 16.102 52.996 1.00 35.01 7038 OW0 WAT W 833 80.371 −18.513 48.901 1.00 45.56 7039 OW0 WAT W 834 64.966 −13.780 2.163 1.00 45.15 7040 OW0 WAT W 835 90.651 −7.000 22.378 1.00 39.28 7041 OW0 WAT W 836 70.311 5.553 14.709 1.00 31.82 7042 OW0 WAT W 837 45.088 24.790 51.597 1.00 50.96 7043 OW0 WAT W 838 65.259 23.437 36.483 1.00 58.46 7044 OW0 WAT W 839 23.969 −18.104 −13.469 1.00 44.45 7045 OW0 WAT W 840 98.275 −11.384 39.798 1.00 40.16 7046 OW0 WAT W 841 43.468 −4.550 50.159 1.00 42.27 7047 OW0 WAT W 842 55.531 24.997 41.758 1.00 43.49 7048 OW0 WAT W 843 79.423 −25.689 −0.377 1.00 50.83 7049 OW0 WAT W 844 82.729 −5.447 14.530 1.00 37.55 7050 OW0 WAT W 845 57.277 −20.688 32.754 1.00 27.47 7051 OW0 WAT W 846 34.927 18.980 47.765 1.00 43.87 7052 OW0 WAT W 847 66.697 21.490 33.750 1.00 55.52 7053 OW0 WAT W 848 52.866 −18.940 42.635 1.00 48.02 7054 OW0 WAT W 849 50.290 −12.920 19.561 1.00 49.79 7055 OW0 WAT W 850 24.446 5.767 29.203 1.00 39.68 7056 OW0 WAT W 851 44.555 9.373 55.910 1.00 30.53 7057 OW0 WAT W 852 59.190 7.201 65.033 1.00 43.41 7058 OW0 WAT W 853 23.010 7.765 61.451 1.00 52.83 7059 OW0 WAT W 854 22.922 24.189 36.031 1.00 41.20 7060 OW0 WAT W 855 57.790 −3.694 56.332 1.00 51.83 7061 OW0 WAT W 856 23.937 14.064 59.101 1.00 46.09 7062 OW0 WAT W 857 65.116 20.932 49.254 1.00 41.13 7063 OW0 WAT W 858 38.488 17.732 55.214 1.00 40.12 7064 OW0 WAT W 859 39.060 7.114 −23.052 1.00 31.07 7065 OW0 WAT W 860 44.261 9.954 −10.440 1.00 45.44 7066 OW0 WAT W 861 57.678 24.011 45.961 1.00 35.78 7067 OW0 WAT W 862 62.731 −18.645 24.010 1.00 34.48 7068 OW0 WAT W 863 55.872 23.413 49.005 1.00 52.80 7069 OW0 WAT W 864 78.578 2.825 2.653 1.00 47.81 7070 OW0 WAT W 865 82.130 −6.162 9.951 1.00 45.86 7071 OW0 WAT W 866 69.803 −18.155 38.558 1.00 50.20 7072 OW0 WAT W 867 11.916 7.726 43.912 1.00 34.68 END      867 11.916 7.726 43.912 1.00 34.68

APPENDIX 2 1                                                   50 50 Promozyme DSTSTKVIVH YHRFDSNYTN WDVWMWPYQP VNGNGAAYQF TGTNDDFGAV B.acidopul DSTSTEVIVH YHRFDSNYAN WDLWMWPYQP VNGNGAAYEF SG.KDDFGVK B.deramifi DGNTTTIIVH YFRPAGDYQP WSLWMW...P KDGGGAEYDF NQPADSFGAV 51                                                 100 Promozyme ADTQVPGDNT QVGLIVRKND WSEKNTPNDL HIDLAKGHEV WIVQGDPTIY B.acidopul ADVQVPGDDT QVGLIVRTND WSQKNTSDDL HIDLTKGHEI WIVQGDPNIY B.deramifi ASADIPGNPS QVGIIVRTQD WT.KDVSADR YIDLSKGNEV WLVEGNSQIF 101                                                150 Promozyme YNLSDAQAAA IPSVSNAYLD DEKTVLAKLS MPMTLADAAS GFTVIDKTTG B.acidopul YNLSDAQAAA TPKVSNAYLD NEKTVLAKLT NPMTLSDGSS GFTVTDKTTG B.deramifi YNEKDAEDAA KPAVSNAYLD ASNQVLVKLS QPLTLGEGAS GFTVHDDTAN 151                                                197 Promozyme EKIPVTSAVS A...NPVTAV LVGDLQQALG AANNWSPDDD HTLLKKINPN B.acidopul EQIPVTAATN A...NS.... .......... .......... .......... B.deramifi KDIPVTSVKD ASLGQDVTAV LAGTFQHIFG GS.DWAPDNH STLLKKVTNN 198                                                246 Promozyme LYQLSGTLPA GTYQYKIALD HSW.NTSYPG NNVSLTVPQG GEKVTFTYIP B.acidopul .......... .......... .......... .......... .......... B.deramifi LYQFSGDLPE GNYQYKVALN DSWNNPSYPS DNINLTVPAG GAHVTFSYIP 247                                                296 Promozyme STNQVFDSVN HPNQAFPTSS AGVQTNLVQL TLASAPDVTH NLDVAADGYK B.acidopul .......... ........AS SSEQTDLVQL TLASAPDVSH TIQVGAAGYE B.deramifi STHAVYDTIN NPNADLQVES .GVKTDLVTV TLGEDPDVSH TLSIQTDGYQ 297                                                346 Promozyme AHNILPRNVL NLPRYDYSGN DLGNVYSKDA TSFRVWAPTA SNVQLLLYNS B.acidopul AVNLIPRNVL NLPRYYYSGN DLGNVYSNKA TAFRVWAPTA SDVQLLLYNS B.deramifi AKQVIPRNVL NSSQYYYSGD DLGNTYTQKA TTFKVWAPTS TQVNVLLYDS 347                                                396 Promozyme EKGSITKQLE MQKSDNGTWK LQVSGNLENW YYLYQVTVNG TTQTAVDPYA B.acidopul ETGPVTKQLE MQKSDNGTWK LKVPGNLKNW YYLYQVTVNG KTQTAVDPYV B.deramifi ATGSVTKIVP MTASGHGVWE ATVNQNLENW YYMYEVTGQG STRTAVDPYA 397                                                446 Promozyme RAISVNATRG MIVDLKATDP AGWQGDHEQT PANPVDEVIY EAHVRDFSID B.acidopul RAISVNATRG MIVDLEDTNP PGWKEDHQQT PANPVDEVIY EVHVRDFSID B.deramifi TAIAPNGTRG MIVDLAKTDP AGWNSDKHIT PKNIEDEVIY EMDVRDFSID 447                                                496 Promozyme ANSGMKNKGK YLAFTEHGTK GPDHVKTGID SLKELGITTV QLQPVEEFNS B.acidopul ANSGMKNKGK YLAFTEHGTK GPDNVKTGID SLKELGINAV QLQPIEEFNS B.deramifi PNSGMKNKGK YLALTEKGTK GPDNVKTGID SLKQLGITHV QLMPVFASNS 497                                                546 Promozyme IDETQPDTYN WGYDPRNYNV PEGAYATTPE GTARITELKQ LIQSLHQQRI B.acidopul IDETQPNMYN WGYDFRNYNV PEGAYATTPE GTARITQLKQ LIQSIHKDRI B.deramifi VDETDPTQDN WGYDPRNYDV PEGQYATNAN GNARIKEFKE MVLSLHREHI 547                                                596 Promozyme GVNMDVVYNH TFDVMVSDFD KIVPQYYYRT DSNGNYTNGS GCGNEFATEH B.acidopul AINMDVVYNH TFNVGVSDFD KIVPQYYYRT DSAGNYTNGS GVGNEIATER B.deramifi GVNMDVVYNH TFATQISDFD KIVPEYYYRT DDAGNYTNGS GTGNEIAAER 597                                                646 Promozyme PMAQKFVLDS VNYWVNEYHV DGFRFDLMAL LGKDTMAKIS NELHAINPGI B.acidopul PMVQKFVLDS VKYWVKEYHI DGFRFDLMAL LGKDTMAKIS KELHAINPGI B.deramifi PMVQKFIIDS LKYWVNEYHI DGFRFDLMAL LGKDTMSKAA SELHAINPGI 647                                                696 Promozyme VLYGEPWTGG TSGLSSDQLV TKGQQKGLGI GVFNDNIRNG LDGNVFDKTA B.acidopul VLYGEPWTGG TSGLSSDQLV TKGQQKGLGI GVFNDNIRNG LDGNVFDKSA B.deramifi ALYGEPWTGG TSALPDDQLL TKGAQKGMGV AVFNDNLRNA LDGNVFDSSA 697                                                746 Promozyme QGFATGDPNQ VDVIKNGVIG SIQDFTSAPS ETINYVTSHD NMTLWDKILA B.acidopul QGFATGDPNQ VNVIKNRVMG SISDFTSAPS ETINYVTSHD NMTLWDKISA B.deramifi QGFATGATGL TDAIKNGVEG SINDFTSSPG ETINYVTSHD NYTLWDKIAL 747                                                796 Promozyme SNPSDTEADR IKMDELAHAV VFTSQGVPFM QGGEEMLRTK GGNDNSYNAG B.acidopul SNPNDTQADR IKMDELAQAV VFTSQGVPFM QGGEEMLRTK GGNDNSYNAG B.deramifi SNPNDSEADR IKMDELAQAV VMTSQGVPFM QGGEEMLRTK GGNDNSYNAG 797                                                846 Promozyme DSVNQFDWSR KAQFKDVFDY FSSMIHLRNQ HPAFRMTTAD QIKQNLTFLE B.acidopul DSVNQFDWSR KAQFENVFDY YSWLIHLRDN HPAFRMTTAD QIKQNLTFLD B.deramifi DAVNEFDWSR KAQYPDVFNY YSGLIHLRLD HPAFRMTTAN EINSHLQFLN 847                                                896 Promozyme SPTNTVAFEL KNYANHDTWK NIIVMYNPNK TSQTLNLPSG DWTIVGLGDQ B.acidopul SPTNTVAFEL KNHANHDKWK NIIVMYNPNK TAQTLTLPSG NWTIVGLGNQ B.deramifi SPENTVAYEL TDHVNKDKWG NIIVVYNPNK TVATINLPSG KWAINATSGK 897                       921 Promozyme IGEKSLGHVM GNVQVPAIST LILKQ..... ..... B.acidopul VGEKSLGHVN GTVEVPALST IILHQGTSED VIDQN B.deramifi VGESTLGQAE GSVQVPGISM MILHQEVSPD HGKK.

10 1 2766 DNA Bacillus acidopullulyticus CDS (1)...(2763) 1 gat tct act tcg act aaa gtt att gtt cat tat cat cgt ttt gat tcc 48 Asp Ser Thr Ser Thr Lys Val Ile Val His Tyr His Arg Phe Asp Ser 1 5 10 15 aac tat acg aat tgg gac gtc tgg atg tgg cct tat cag cct gtt aat 96 Asn Tyr Thr Asn Trp Asp Val Trp Met Trp Pro Tyr Gln Pro Val Asn 20 25 30 ggt aat gga gca gct tac caa ttc act ggt aca aat gat gat ttt ggc 144 Gly Asn Gly Ala Ala Tyr Gln Phe Thr Gly Thr Asn Asp Asp Phe Gly 35 40 45 gct gtt gca gat acg caa gtg cct gga gat aat aca caa gtt ggt ttg 192 Ala Val Ala Asp Thr Gln Val Pro Gly Asp Asn Thr Gln Val Gly Leu 50 55 60 att gtt cgt aaa aat gat tgg agc gag aaa aat aca cca aac gat ctc 240 Ile Val Arg Lys Asn Asp Trp Ser Glu Lys Asn Thr Pro Asn Asp Leu 65 70 75 80 cat att gac ctt gca aaa ggc cat gaa gta tgg att gta caa ggg gat 288 His Ile Asp Leu Ala Lys Gly His Glu Val Trp Ile Val Gln Gly Asp 85 90 95 cca act att tat tac aat ctg agc gac gca cag gct gcc gca ata cca 336 Pro Thr Ile Tyr Tyr Asn Leu Ser Asp Ala Gln Ala Ala Ala Ile Pro 100 105 110 tct gtt tca aat gcc tat ctt gat gat gaa aaa aca gta cta gca aag 384 Ser Val Ser Asn Ala Tyr Leu Asp Asp Glu Lys Thr Val Leu Ala Lys 115 120 125 cta agt atg ccg atg acg ctg gcg gat gct gca agc ggc ttt acg gtt 432 Leu Ser Met Pro Met Thr Leu Ala Asp Ala Ala Ser Gly Phe Thr Val 130 135 140 ata gat aaa acc aca ggt gaa aaa atc cct gtc acc tct gct gta tcc 480 Ile Asp Lys Thr Thr Gly Glu Lys Ile Pro Val Thr Ser Ala Val Ser 145 150 155 160 gca aat ccg gta act gcc gtt ctt gtt gga gat tta caa cag gct ttg 528 Ala Asn Pro Val Thr Ala Val Leu Val Gly Asp Leu Gln Gln Ala Leu 165 170 175 gga gca gcg aat aat tgg tca cca gat gat gat cac aca ctg cta aaa 576 Gly Ala Ala Asn Asn Trp Ser Pro Asp Asp Asp His Thr Leu Leu Lys 180 185 190 aag ata aat cca aac ctt tac caa tta tcg ggg aca ctt cca gct ggt 624 Lys Ile Asn Pro Asn Leu Tyr Gln Leu Ser Gly Thr Leu Pro Ala Gly 195 200 205 aca tac caa tat aag ata gcc ttg gac cat tct tgg aat acc tcc tat 672 Thr Tyr Gln Tyr Lys Ile Ala Leu Asp His Ser Trp Asn Thr Ser Tyr 210 215 220 cca ggt aac aat gta agt ctt act gtt cct cag gga ggg gaa aag gtt 720 Pro Gly Asn Asn Val Ser Leu Thr Val Pro Gln Gly Gly Glu Lys Val 225 230 235 240 acc ttt acc tat att cca tct acc aac cag gta ttc gat agc gtc aat 768 Thr Phe Thr Tyr Ile Pro Ser Thr Asn Gln Val Phe Asp Ser Val Asn 245 250 255 cat cct aac caa gca ttc cct aca tcc tca gca ggg gtc cag aca aat 816 His Pro Asn Gln Ala Phe Pro Thr Ser Ser Ala Gly Val Gln Thr Asn 260 265 270 tta gtc caa ttg act tta gcg agt gca ccg gat gtc acc cat aat tta 864 Leu Val Gln Leu Thr Leu Ala Ser Ala Pro Asp Val Thr His Asn Leu 275 280 285 gat gta gca gca gac ggt tac aaa gcg cac aat att tta cca agg aat 912 Asp Val Ala Ala Asp Gly Tyr Lys Ala His Asn Ile Leu Pro Arg Asn 290 295 300 gtt tta aat ctg ccg cgg tat gat tat agt gga aat gat ttg ggt aat 960 Val Leu Asn Leu Pro Arg Tyr Asp Tyr Ser Gly Asn Asp Leu Gly Asn 305 310 315 320 gtt tat tca aag gat gca aca tcc ttc cgg gta tgg gct cca aca gct 1008 Val Tyr Ser Lys Asp Ala Thr Ser Phe Arg Val Trp Ala Pro Thr Ala 325 330 335 tcg aat gtc cag ttg ctt tta tac aat agt gag aaa ggt tca ata act 1056 Ser Asn Val Gln Leu Leu Leu Tyr Asn Ser Glu Lys Gly Ser Ile Thr 340 345 350 aaa cag ctt gaa atg caa aag agt gat aac ggt aca tgg aaa ctt cag 1104 Lys Gln Leu Glu Met Gln Lys Ser Asp Asn Gly Thr Trp Lys Leu Gln 355 360 365 gtt tct ggt aat ctt gaa aac tgg tat tat cta tat caa gtc aca gtg 1152 Val Ser Gly Asn Leu Glu Asn Trp Tyr Tyr Leu Tyr Gln Val Thr Val 370 375 380 aat ggg aca aca caa acg gca gtt gat cca tat gcg cgt gct att tct 1200 Asn Gly Thr Thr Gln Thr Ala Val Asp Pro Tyr Ala Arg Ala Ile Ser 385 390 395 400 gtc aat gca aca cgc ggt atg att gtg gac cta aaa gct acc gat cct 1248 Val Asn Ala Thr Arg Gly Met Ile Val Asp Leu Lys Ala Thr Asp Pro 405 410 415 gca ggg tgg cag gga gat cat gaa cag aca cct gcg aat cca gta gat 1296 Ala Gly Trp Gln Gly Asp His Glu Gln Thr Pro Ala Asn Pro Val Asp 420 425 430 gaa gtg att tat gaa gcg cat gta cgc gat ttt tcg att gat gct aat 1344 Glu Val Ile Tyr Glu Ala His Val Arg Asp Phe Ser Ile Asp Ala Asn 435 440 445 tca ggt atg aaa aat aaa ggg aag tat tta gcg ttt aca gag cat gga 1392 Ser Gly Met Lys Asn Lys Gly Lys Tyr Leu Ala Phe Thr Glu His Gly 450 455 460 aca aaa gga ccg gat cat gta aag aca ggt att gat agt ttg aag gaa 1440 Thr Lys Gly Pro Asp His Val Lys Thr Gly Ile Asp Ser Leu Lys Glu 465 470 475 480 ttg ggc atc acc act gtt caa ttg caa cct gtt gag gag ttt aac agt 1488 Leu Gly Ile Thr Thr Val Gln Leu Gln Pro Val Glu Glu Phe Asn Ser 485 490 495 att gat gag acc cag cct gat acg tat aac tgg ggc tac gat cca agg 1536 Ile Asp Glu Thr Gln Pro Asp Thr Tyr Asn Trp Gly Tyr Asp Pro Arg 500 505 510 aac tat aac gta cca gag gga gct tat gcc aca act cca gaa gga aca 1584 Asn Tyr Asn Val Pro Glu Gly Ala Tyr Ala Thr Thr Pro Glu Gly Thr 515 520 525 gcg cgt ata aca gaa tta aag caa tta att caa agc ctt cat cag cag 1632 Ala Arg Ile Thr Glu Leu Lys Gln Leu Ile Gln Ser Leu His Gln Gln 530 535 540 cgg att ggt gtc aat atg gat gtt gtt tat aac cat acc ttt gat gtg 1680 Arg Ile Gly Val Asn Met Asp Val Val Tyr Asn His Thr Phe Asp Val 545 550 555 560 atg gtt tct gat ttt gat aaa att gtc ccg caa tat tat tat cgt acc 1728 Met Val Ser Asp Phe Asp Lys Ile Val Pro Gln Tyr Tyr Tyr Arg Thr 565 570 575 gat agt aat ggc aat tat acg aac gga tca ggt tgc ggc aat gaa ttc 1776 Asp Ser Asn Gly Asn Tyr Thr Asn Gly Ser Gly Cys Gly Asn Glu Phe 580 585 590 gcg act gag cat cca atg gca caa aag ttt gtg ctt gat tca gtt aat 1824 Ala Thr Glu His Pro Met Ala Gln Lys Phe Val Leu Asp Ser Val Asn 595 600 605 tat tgg gta aat gag tac cac gtg gat ggc ttc cgt ttt gac tta atg 1872 Tyr Trp Val Asn Glu Tyr His Val Asp Gly Phe Arg Phe Asp Leu Met 610 615 620 gct ctt tta gga aaa gac acg atg gca aaa ata tca aac gag ctg cat 1920 Ala Leu Leu Gly Lys Asp Thr Met Ala Lys Ile Ser Asn Glu Leu His 625 630 635 640 gcc att aat cct ggt att gtt tta tat gga gaa cca tgg act ggc ggc 1968 Ala Ile Asn Pro Gly Ile Val Leu Tyr Gly Glu Pro Trp Thr Gly Gly 645 650 655 aca tcg gga tta tct agc gac cag ctt gta acg aag ggt caa caa aag 2016 Thr Ser Gly Leu Ser Ser Asp Gln Leu Val Thr Lys Gly Gln Gln Lys 660 665 670 gga tta gga att ggc gtt ttc aac gat aat ata cgt aat ggg ctc gat 2064 Gly Leu Gly Ile Gly Val Phe Asn Asp Asn Ile Arg Asn Gly Leu Asp 675 680 685 ggg aac gtg ttt gat aaa acg gca caa ggc ttt gca aca gga gat cca 2112 Gly Asn Val Phe Asp Lys Thr Ala Gln Gly Phe Ala Thr Gly Asp Pro 690 695 700 aac cag gtg gat gtc att aaa aat gga gta atc ggt agt att caa gat 2160 Asn Gln Val Asp Val Ile Lys Asn Gly Val Ile Gly Ser Ile Gln Asp 705 710 715 720 ttt act tca gca cct agc gaa acg att aac tat gtt aca agc cat gat 2208 Phe Thr Ser Ala Pro Ser Glu Thr Ile Asn Tyr Val Thr Ser His Asp 725 730 735 aac atg acg ctt tgg gat aaa att tta gca agt aat cca agt gac act 2256 Asn Met Thr Leu Trp Asp Lys Ile Leu Ala Ser Asn Pro Ser Asp Thr 740 745 750 gag gct gac cga att aaa atg gat gaa ttg gca cat gcc gta gta ttc 2304 Glu Ala Asp Arg Ile Lys Met Asp Glu Leu Ala His Ala Val Val Phe 755 760 765 act tca caa ggt gta cca ttt atg caa ggt gga gaa gaa atg ctg agg 2352 Thr Ser Gln Gly Val Pro Phe Met Gln Gly Gly Glu Glu Met Leu Arg 770 775 780 aca aaa ggc gga aat gat aac agt tat aac gct gga gat agt gtg aat 2400 Thr Lys Gly Gly Asn Asp Asn Ser Tyr Asn Ala Gly Asp Ser Val Asn 785 790 795 800 cag ttc gac tgg tca aga aag gcg caa ttt aag gat gtt ttt gac tac 2448 Gln Phe Asp Trp Ser Arg Lys Ala Gln Phe Lys Asp Val Phe Asp Tyr 805 810 815 ttt tct agt atg att cat ctt cgt aat cag cac ccg gca ttc agg atg 2496 Phe Ser Ser Met Ile His Leu Arg Asn Gln His Pro Ala Phe Arg Met 820 825 830 acg aca gcg gat caa att aaa cag aat ctt aca ttc tta gaa agc cca 2544 Thr Thr Ala Asp Gln Ile Lys Gln Asn Leu Thr Phe Leu Glu Ser Pro 835 840 845 aca aac acg gta gct ttc gag tta aag aat tat gca aac cat gat aca 2592 Thr Asn Thr Val Ala Phe Glu Leu Lys Asn Tyr Ala Asn His Asp Thr 850 855 860 tgg aaa aat ata att gtc atg tat aac cca aat aag act tcc caa acc 2640 Trp Lys Asn Ile Ile Val Met Tyr Asn Pro Asn Lys Thr Ser Gln Thr 865 870 875 880 ctt aat cta cca agt gga gat tgg acc att gta gga ttg gga gat caa 2688 Leu Asn Leu Pro Ser Gly Asp Trp Thr Ile Val Gly Leu Gly Asp Gln 885 890 895 ata ggt gag aaa tca tta ggg cat gta atg ggt aat gtt caa gta ccg 2736 Ile Gly Glu Lys Ser Leu Gly His Val Met Gly Asn Val Gln Val Pro 900 905 910 gct ata agt acg ctt att ctc aaa caa taa 2766 Ala Ile Ser Thr Leu Ile Leu Lys Gln 915 920 2 921 PRT Bacillus acidopullulyticus 2 Asp Ser Thr Ser Thr Lys Val Ile Val His Tyr His Arg Phe Asp Ser 1 5 10 15 Asn Tyr Thr Asn Trp Asp Val Trp Met Trp Pro Tyr Gln Pro Val Asn 20 25 30 Gly Asn Gly Ala Ala Tyr Gln Phe Thr Gly Thr Asn Asp Asp Phe Gly 35 40 45 Ala Val Ala Asp Thr Gln Val Pro Gly Asp Asn Thr Gln Val Gly Leu 50 55 60 Ile Val Arg Lys Asn Asp Trp Ser Glu Lys Asn Thr Pro Asn Asp Leu 65 70 75 80 His Ile Asp Leu Ala Lys Gly His Glu Val Trp Ile Val Gln Gly Asp 85 90 95 Pro Thr Ile Tyr Tyr Asn Leu Ser Asp Ala Gln Ala Ala Ala Ile Pro 100 105 110 Ser Val Ser Asn Ala Tyr Leu Asp Asp Glu Lys Thr Val Leu Ala Lys 115 120 125 Leu Ser Met Pro Met Thr Leu Ala Asp Ala Ala Ser Gly Phe Thr Val 130 135 140 Ile Asp Lys Thr Thr Gly Glu Lys Ile Pro Val Thr Ser Ala Val Ser 145 150 155 160 Ala Asn Pro Val Thr Ala Val Leu Val Gly Asp Leu Gln Gln Ala Leu 165 170 175 Gly Ala Ala Asn Asn Trp Ser Pro Asp Asp Asp His Thr Leu Leu Lys 180 185 190 Lys Ile Asn Pro Asn Leu Tyr Gln Leu Ser Gly Thr Leu Pro Ala Gly 195 200 205 Thr Tyr Gln Tyr Lys Ile Ala Leu Asp His Ser Trp Asn Thr Ser Tyr 210 215 220 Pro Gly Asn Asn Val Ser Leu Thr Val Pro Gln Gly Gly Glu Lys Val 225 230 235 240 Thr Phe Thr Tyr Ile Pro Ser Thr Asn Gln Val Phe Asp Ser Val Asn 245 250 255 His Pro Asn Gln Ala Phe Pro Thr Ser Ser Ala Gly Val Gln Thr Asn 260 265 270 Leu Val Gln Leu Thr Leu Ala Ser Ala Pro Asp Val Thr His Asn Leu 275 280 285 Asp Val Ala Ala Asp Gly Tyr Lys Ala His Asn Ile Leu Pro Arg Asn 290 295 300 Val Leu Asn Leu Pro Arg Tyr Asp Tyr Ser Gly Asn Asp Leu Gly Asn 305 310 315 320 Val Tyr Ser Lys Asp Ala Thr Ser Phe Arg Val Trp Ala Pro Thr Ala 325 330 335 Ser Asn Val Gln Leu Leu Leu Tyr Asn Ser Glu Lys Gly Ser Ile Thr 340 345 350 Lys Gln Leu Glu Met Gln Lys Ser Asp Asn Gly Thr Trp Lys Leu Gln 355 360 365 Val Ser Gly Asn Leu Glu Asn Trp Tyr Tyr Leu Tyr Gln Val Thr Val 370 375 380 Asn Gly Thr Thr Gln Thr Ala Val Asp Pro Tyr Ala Arg Ala Ile Ser 385 390 395 400 Val Asn Ala Thr Arg Gly Met Ile Val Asp Leu Lys Ala Thr Asp Pro 405 410 415 Ala Gly Trp Gln Gly Asp His Glu Gln Thr Pro Ala Asn Pro Val Asp 420 425 430 Glu Val Ile Tyr Glu Ala His Val Arg Asp Phe Ser Ile Asp Ala Asn 435 440 445 Ser Gly Met Lys Asn Lys Gly Lys Tyr Leu Ala Phe Thr Glu His Gly 450 455 460 Thr Lys Gly Pro Asp His Val Lys Thr Gly Ile Asp Ser Leu Lys Glu 465 470 475 480 Leu Gly Ile Thr Thr Val Gln Leu Gln Pro Val Glu Glu Phe Asn Ser 485 490 495 Ile Asp Glu Thr Gln Pro Asp Thr Tyr Asn Trp Gly Tyr Asp Pro Arg 500 505 510 Asn Tyr Asn Val Pro Glu Gly Ala Tyr Ala Thr Thr Pro Glu Gly Thr 515 520 525 Ala Arg Ile Thr Glu Leu Lys Gln Leu Ile Gln Ser Leu His Gln Gln 530 535 540 Arg Ile Gly Val Asn Met Asp Val Val Tyr Asn His Thr Phe Asp Val 545 550 555 560 Met Val Ser Asp Phe Asp Lys Ile Val Pro Gln Tyr Tyr Tyr Arg Thr 565 570 575 Asp Ser Asn Gly Asn Tyr Thr Asn Gly Ser Gly Cys Gly Asn Glu Phe 580 585 590 Ala Thr Glu His Pro Met Ala Gln Lys Phe Val Leu Asp Ser Val Asn 595 600 605 Tyr Trp Val Asn Glu Tyr His Val Asp Gly Phe Arg Phe Asp Leu Met 610 615 620 Ala Leu Leu Gly Lys Asp Thr Met Ala Lys Ile Ser Asn Glu Leu His 625 630 635 640 Ala Ile Asn Pro Gly Ile Val Leu Tyr Gly Glu Pro Trp Thr Gly Gly 645 650 655 Thr Ser Gly Leu Ser Ser Asp Gln Leu Val Thr Lys Gly Gln Gln Lys 660 665 670 Gly Leu Gly Ile Gly Val Phe Asn Asp Asn Ile Arg Asn Gly Leu Asp 675 680 685 Gly Asn Val Phe Asp Lys Thr Ala Gln Gly Phe Ala Thr Gly Asp Pro 690 695 700 Asn Gln Val Asp Val Ile Lys Asn Gly Val Ile Gly Ser Ile Gln Asp 705 710 715 720 Phe Thr Ser Ala Pro Ser Glu Thr Ile Asn Tyr Val Thr Ser His Asp 725 730 735 Asn Met Thr Leu Trp Asp Lys Ile Leu Ala Ser Asn Pro Ser Asp Thr 740 745 750 Glu Ala Asp Arg Ile Lys Met Asp Glu Leu Ala His Ala Val Val Phe 755 760 765 Thr Ser Gln Gly Val Pro Phe Met Gln Gly Gly Glu Glu Met Leu Arg 770 775 780 Thr Lys Gly Gly Asn Asp Asn Ser Tyr Asn Ala Gly Asp Ser Val Asn 785 790 795 800 Gln Phe Asp Trp Ser Arg Lys Ala Gln Phe Lys Asp Val Phe Asp Tyr 805 810 815 Phe Ser Ser Met Ile His Leu Arg Asn Gln His Pro Ala Phe Arg Met 820 825 830 Thr Thr Ala Asp Gln Ile Lys Gln Asn Leu Thr Phe Leu Glu Ser Pro 835 840 845 Thr Asn Thr Val Ala Phe Glu Leu Lys Asn Tyr Ala Asn His Asp Thr 850 855 860 Trp Lys Asn Ile Ile Val Met Tyr Asn Pro Asn Lys Thr Ser Gln Thr 865 870 875 880 Leu Asn Leu Pro Ser Gly Asp Trp Thr Ile Val Gly Leu Gly Asp Gln 885 890 895 Ile Gly Glu Lys Ser Leu Gly His Val Met Gly Asn Val Gln Val Pro 900 905 910 Ala Ile Ser Thr Leu Ile Leu Lys Gln 915 920 3 2787 DNA Bacillus deramificans CDS (1)...(2784) 3 gat ggg aac acg aca acg atc att gtc cac tat ttt cgc cct gct ggt 48 Asp Gly Asn Thr Thr Thr Ile Ile Val His Tyr Phe Arg Pro Ala Gly 1 5 10 15 gat tat caa cct tgg agt cta tgg atg tgg cca aaa gac gga ggt ggg 96 Asp Tyr Gln Pro Trp Ser Leu Trp Met Trp Pro Lys Asp Gly Gly Gly 20 25 30 gct gaa tac gat ttc aat caa ccg gct gac tct ttt gga gct gtt gca 144 Ala Glu Tyr Asp Phe Asn Gln Pro Ala Asp Ser Phe Gly Ala Val Ala 35 40 45 agt gct gat att cca gga aac cca agt cag gta gga att atc gtt cgc 192 Ser Ala Asp Ile Pro Gly Asn Pro Ser Gln Val Gly Ile Ile Val Arg 50 55 60 act caa gat tgg acc aaa gat gtg agc gct gac cgc tac ata gat tta 240 Thr Gln Asp Trp Thr Lys Asp Val Ser Ala Asp Arg Tyr Ile Asp Leu 65 70 75 80 agc aaa gga aat gag gtg tgg ctt gta gaa gga aac agc caa att ttt 288 Ser Lys Gly Asn Glu Val Trp Leu Val Glu Gly Asn Ser Gln Ile Phe 85 90 95 tat aat gaa aaa gat gct gag gat gca gct aaa ccc gct gta agc aac 336 Tyr Asn Glu Lys Asp Ala Glu Asp Ala Ala Lys Pro Ala Val Ser Asn 100 105 110 gct tat tta gat gct tca aac cag gtg ctg gtt aaa ctt agc cag ccg 384 Ala Tyr Leu Asp Ala Ser Asn Gln Val Leu Val Lys Leu Ser Gln Pro 115 120 125 tta act ctt ggg gaa ggc gca agc ggc ttt acg gtt cat gac gac aca 432 Leu Thr Leu Gly Glu Gly Ala Ser Gly Phe Thr Val His Asp Asp Thr 130 135 140 gca aat aag gat att cca gtg aca tct gtg aag gat gca agt ctt ggt 480 Ala Asn Lys Asp Ile Pro Val Thr Ser Val Lys Asp Ala Ser Leu Gly 145 150 155 160 caa gat gta acc gct gtt ttg gca ggt acc ttc caa cat att ttt gga 528 Gln Asp Val Thr Ala Val Leu Ala Gly Thr Phe Gln His Ile Phe Gly 165 170 175 ggt tcc gat tgg gca cct gat aat cac agt act tta tta aaa aag gtg 576 Gly Ser Asp Trp Ala Pro Asp Asn His Ser Thr Leu Leu Lys Lys Val 180 185 190 act aac aat ctc tat caa ttc tca gga gat ctt cct gaa gga aac tac 624 Thr Asn Asn Leu Tyr Gln Phe Ser Gly Asp Leu Pro Glu Gly Asn Tyr 195 200 205 caa tat aaa gtg gct tta aat gat agc tgg aat aat ccg agt tac cca 672 Gln Tyr Lys Val Ala Leu Asn Asp Ser Trp Asn Asn Pro Ser Tyr Pro 210 215 220 tct gac aac att aat tta aca gtc cct gcc ggc ggt gca cac gtc act 720 Ser Asp Asn Ile Asn Leu Thr Val Pro Ala Gly Gly Ala His Val Thr 225 230 235 240 ttt tcg tat att ccg tcc act cat gca gtc tat gac aca att aat aat 768 Phe Ser Tyr Ile Pro Ser Thr His Ala Val Tyr Asp Thr Ile Asn Asn 245 250 255 cct aat gcg gat tta caa gta gaa agc ggg gtt aaa acg gat ctc gtg 816 Pro Asn Ala Asp Leu Gln Val Glu Ser Gly Val Lys Thr Asp Leu Val 260 265 270 acg gtt act cta ggg gaa gat cca gat gtg agc cat act ctg tcc att 864 Thr Val Thr Leu Gly Glu Asp Pro Asp Val Ser His Thr Leu Ser Ile 275 280 285 caa aca gat ggc tat cag gca aag cag gtg ata cct cgt aat gtg ctt 912 Gln Thr Asp Gly Tyr Gln Ala Lys Gln Val Ile Pro Arg Asn Val Leu 290 295 300 aat tca tca cag tac tac tat tca gga gat gat ctt ggg aat acc tat 960 Asn Ser Ser Gln Tyr Tyr Tyr Ser Gly Asp Asp Leu Gly Asn Thr Tyr 305 310 315 320 aca cag aaa gca aca acc ttt aaa gtc tgg gca cca act tct act caa 1008 Thr Gln Lys Ala Thr Thr Phe Lys Val Trp Ala Pro Thr Ser Thr Gln 325 330 335 gta aat gtt ctt ctt tat gac agt gca acg ggt tct gta aca aaa atc 1056 Val Asn Val Leu Leu Tyr Asp Ser Ala Thr Gly Ser Val Thr Lys Ile 340 345 350 gta cct atg acg gca tcg ggc cat ggt gtg tgg gaa gca acg gtt aat 1104 Val Pro Met Thr Ala Ser Gly His Gly Val Trp Glu Ala Thr Val Asn 355 360 365 caa aac ctt gaa aat tgg tat tac atg tat gag gta aca ggc caa ggc 1152 Gln Asn Leu Glu Asn Trp Tyr Tyr Met Tyr Glu Val Thr Gly Gln Gly 370 375 380 tct acc cga acg gct gtt gat cct tat gca act gcg att gca cca aat 1200 Ser Thr Arg Thr Ala Val Asp Pro Tyr Ala Thr Ala Ile Ala Pro Asn 385 390 395 400 gga acg aga ggc atg att gtg gac ctg gct aaa aca gat cct gct ggc 1248 Gly Thr Arg Gly Met Ile Val Asp Leu Ala Lys Thr Asp Pro Ala Gly 405 410 415 tgg aac agt gat aaa cat att acg cca aag aat ata gaa gat gag gtc 1296 Trp Asn Ser Asp Lys His Ile Thr Pro Lys Asn Ile Glu Asp Glu Val 420 425 430 atc tat gaa atg gat gtc cgt gac ttt tcc att gac cct aat tcg ggt 1344 Ile Tyr Glu Met Asp Val Arg Asp Phe Ser Ile Asp Pro Asn Ser Gly 435 440 445 atg aaa aat aaa ggg aag tat ttg gct ctt aca gaa aaa gga aca aag 1392 Met Lys Asn Lys Gly Lys Tyr Leu Ala Leu Thr Glu Lys Gly Thr Lys 450 455 460 ggc cct gac aac gta aag acg ggg ata gat tcc tta aaa caa ctt ggg 1440 Gly Pro Asp Asn Val Lys Thr Gly Ile Asp Ser Leu Lys Gln Leu Gly 465 470 475 480 att act cat gtt cag ctt atg cct gtt ttc gca tct aac agt gtc gat 1488 Ile Thr His Val Gln Leu Met Pro Val Phe Ala Ser Asn Ser Val Asp 485 490 495 gaa act gat cca acc caa gat aat tgg ggt tat gac cct cgc aac tat 1536 Glu Thr Asp Pro Thr Gln Asp Asn Trp Gly Tyr Asp Pro Arg Asn Tyr 500 505 510 gat gtt cct gaa ggg cag tat gct aca aat gcg aat ggt aat gct cgt 1584 Asp Val Pro Glu Gly Gln Tyr Ala Thr Asn Ala Asn Gly Asn Ala Arg 515 520 525 ata aaa gag ttt aag gaa atg gtt ctt tca ctc cat cgt gaa cac att 1632 Ile Lys Glu Phe Lys Glu Met Val Leu Ser Leu His Arg Glu His Ile 530 535 540 ggg gtt aac atg gat gtt gtc tat aat cat acc ttt gcc acg caa atc 1680 Gly Val Asn Met Asp Val Val Tyr Asn His Thr Phe Ala Thr Gln Ile 545 550 555 560 tct gac ttc gat aaa att gta cca gaa tat tat tac cgt acg gat gat 1728 Ser Asp Phe Asp Lys Ile Val Pro Glu Tyr Tyr Tyr Arg Thr Asp Asp 565 570 575 gca ggt aat tat acc aac gga tca ggt act gga aat gaa att gca gcc 1776 Ala Gly Asn Tyr Thr Asn Gly Ser Gly Thr Gly Asn Glu Ile Ala Ala 580 585 590 gaa agg cca atg gtt caa aaa ttt att att gat tcc ctt aag tat tgg 1824 Glu Arg Pro Met Val Gln Lys Phe Ile Ile Asp Ser Leu Lys Tyr Trp 595 600 605 gtc aat gag tat cat att gac ggc ttc cgt ttt gac tta atg gcg ctg 1872 Val Asn Glu Tyr His Ile Asp Gly Phe Arg Phe Asp Leu Met Ala Leu 610 615 620 ctt gga aaa gac acg atg tcc aaa gct gcc tcg gag ctt cat gct att 1920 Leu Gly Lys Asp Thr Met Ser Lys Ala Ala Ser Glu Leu His Ala Ile 625 630 635 640 aat cca gga att gca ctt tac ggt gag cca tgg acg ggt gga acc tct 1968 Asn Pro Gly Ile Ala Leu Tyr Gly Glu Pro Trp Thr Gly Gly Thr Ser 645 650 655 gca ctg cca gat gat cag ctt ctg aca aaa gga gct caa aaa ggc atg 2016 Ala Leu Pro Asp Asp Gln Leu Leu Thr Lys Gly Ala Gln Lys Gly Met 660 665 670 gga gta gcg gtg ttt aat gac aat tta cga aac gcg ttg gac ggc aat 2064 Gly Val Ala Val Phe Asn Asp Asn Leu Arg Asn Ala Leu Asp Gly Asn 675 680 685 gtc ttt gat tct tcc gct caa ggt ttt gcg aca ggt gca aca ggc tta 2112 Val Phe Asp Ser Ser Ala Gln Gly Phe Ala Thr Gly Ala Thr Gly Leu 690 695 700 act gat gca att aag aat ggc gtt gag ggg agt att aat gac ttt acc 2160 Thr Asp Ala Ile Lys Asn Gly Val Glu Gly Ser Ile Asn Asp Phe Thr 705 710 715 720 tct tca cca ggt gag aca att aac tat gtc aca agt cat gat aac tac 2208 Ser Ser Pro Gly Glu Thr Ile Asn Tyr Val Thr Ser His Asp Asn Tyr 725 730 735 acc ctt tgg gac aaa ata gcc cta agc aat cct aat gat tcc gaa gcg 2256 Thr Leu Trp Asp Lys Ile Ala Leu Ser Asn Pro Asn Asp Ser Glu Ala 740 745 750 gat cgg att aaa atg gat gaa ctc gca caa gca gtt gtt atg acc tca 2304 Asp Arg Ile Lys Met Asp Glu Leu Ala Gln Ala Val Val Met Thr Ser 755 760 765 caa ggc gtt cca ttc atg caa ggc ggg gaa gaa atg ctt cgt aca aaa 2352 Gln Gly Val Pro Phe Met Gln Gly Gly Glu Glu Met Leu Arg Thr Lys 770 775 780 ggc ggc aac gac aat agt tat aat gca ggc gat gcg gtc aat gag ttt 2400 Gly Gly Asn Asp Asn Ser Tyr Asn Ala Gly Asp Ala Val Asn Glu Phe 785 790 795 800 gat tgg agc agg aaa gct caa tat cca gat gtt ttc aac tat tat agc 2448 Asp Trp Ser Arg Lys Ala Gln Tyr Pro Asp Val Phe Asn Tyr Tyr Ser 805 810 815 ggg cta atc cac ctt cgt ctt gat cac cca gcc ttc cgc atg acg aca 2496 Gly Leu Ile His Leu Arg Leu Asp His Pro Ala Phe Arg Met Thr Thr 820 825 830 gct aat gaa atc aat agc cac ctc caa ttc cta aat agt cca gag aac 2544 Ala Asn Glu Ile Asn Ser His Leu Gln Phe Leu Asn Ser Pro Glu Asn 835 840 845 aca gtg gcc tat gaa tta act gat cat gtt aat aaa gac aaa tgg gga 2592 Thr Val Ala Tyr Glu Leu Thr Asp His Val Asn Lys Asp Lys Trp Gly 850 855 860 aat atc att gtt gtt tat aac cca aat aaa act gta gca acc atc aat 2640 Asn Ile Ile Val Val Tyr Asn Pro Asn Lys Thr Val Ala Thr Ile Asn 865 870 875 880 ttg ccg agc ggg aaa tgg gca atc aat gct acg agc ggt aag gta gga 2688 Leu Pro Ser Gly Lys Trp Ala Ile Asn Ala Thr Ser Gly Lys Val Gly 885 890 895 gaa tcc acc ctt ggt caa gca gag gga agt gtc caa gta cca ggt ata 2736 Glu Ser Thr Leu Gly Gln Ala Glu Gly Ser Val Gln Val Pro Gly Ile 900 905 910 tct atg atg atc ctt cat caa gag gta agc cca gac cac ggt aaa aag 2784 Ser Met Met Ile Leu His Gln Glu Val Ser Pro Asp His Gly Lys Lys 915 920 925 taa 2787 4 928 PRT Bacillus deramificans 4 Asp Gly Asn Thr Thr Thr Ile Ile Val His Tyr Phe Arg Pro Ala Gly 1 5 10 15 Asp Tyr Gln Pro Trp Ser Leu Trp Met Trp Pro Lys Asp Gly Gly Gly 20 25 30 Ala Glu Tyr Asp Phe Asn Gln Pro Ala Asp Ser Phe Gly Ala Val Ala 35 40 45 Ser Ala Asp Ile Pro Gly Asn Pro Ser Gln Val Gly Ile Ile Val Arg 50 55 60 Thr Gln Asp Trp Thr Lys Asp Val Ser Ala Asp Arg Tyr Ile Asp Leu 65 70 75 80 Ser Lys Gly Asn Glu Val Trp Leu Val Glu Gly Asn Ser Gln Ile Phe 85 90 95 Tyr Asn Glu Lys Asp Ala Glu Asp Ala Ala Lys Pro Ala Val Ser Asn 100 105 110 Ala Tyr Leu Asp Ala Ser Asn Gln Val Leu Val Lys Leu Ser Gln Pro 115 120 125 Leu Thr Leu Gly Glu Gly Ala Ser Gly Phe Thr Val His Asp Asp Thr 130 135 140 Ala Asn Lys Asp Ile Pro Val Thr Ser Val Lys Asp Ala Ser Leu Gly 145 150 155 160 Gln Asp Val Thr Ala Val Leu Ala Gly Thr Phe Gln His Ile Phe Gly 165 170 175 Gly Ser Asp Trp Ala Pro Asp Asn His Ser Thr Leu Leu Lys Lys Val 180 185 190 Thr Asn Asn Leu Tyr Gln Phe Ser Gly Asp Leu Pro Glu Gly Asn Tyr 195 200 205 Gln Tyr Lys Val Ala Leu Asn Asp Ser Trp Asn Asn Pro Ser Tyr Pro 210 215 220 Ser Asp Asn Ile Asn Leu Thr Val Pro Ala Gly Gly Ala His Val Thr 225 230 235 240 Phe Ser Tyr Ile Pro Ser Thr His Ala Val Tyr Asp Thr Ile Asn Asn 245 250 255 Pro Asn Ala Asp Leu Gln Val Glu Ser Gly Val Lys Thr Asp Leu Val 260 265 270 Thr Val Thr Leu Gly Glu Asp Pro Asp Val Ser His Thr Leu Ser Ile 275 280 285 Gln Thr Asp Gly Tyr Gln Ala Lys Gln Val Ile Pro Arg Asn Val Leu 290 295 300 Asn Ser Ser Gln Tyr Tyr Tyr Ser Gly Asp Asp Leu Gly Asn Thr Tyr 305 310 315 320 Thr Gln Lys Ala Thr Thr Phe Lys Val Trp Ala Pro Thr Ser Thr Gln 325 330 335 Val Asn Val Leu Leu Tyr Asp Ser Ala Thr Gly Ser Val Thr Lys Ile 340 345 350 Val Pro Met Thr Ala Ser Gly His Gly Val Trp Glu Ala Thr Val Asn 355 360 365 Gln Asn Leu Glu Asn Trp Tyr Tyr Met Tyr Glu Val Thr Gly Gln Gly 370 375 380 Ser Thr Arg Thr Ala Val Asp Pro Tyr Ala Thr Ala Ile Ala Pro Asn 385 390 395 400 Gly Thr Arg Gly Met Ile Val Asp Leu Ala Lys Thr Asp Pro Ala Gly 405 410 415 Trp Asn Ser Asp Lys His Ile Thr Pro Lys Asn Ile Glu Asp Glu Val 420 425 430 Ile Tyr Glu Met Asp Val Arg Asp Phe Ser Ile Asp Pro Asn Ser Gly 435 440 445 Met Lys Asn Lys Gly Lys Tyr Leu Ala Leu Thr Glu Lys Gly Thr Lys 450 455 460 Gly Pro Asp Asn Val Lys Thr Gly Ile Asp Ser Leu Lys Gln Leu Gly 465 470 475 480 Ile Thr His Val Gln Leu Met Pro Val Phe Ala Ser Asn Ser Val Asp 485 490 495 Glu Thr Asp Pro Thr Gln Asp Asn Trp Gly Tyr Asp Pro Arg Asn Tyr 500 505 510 Asp Val Pro Glu Gly Gln Tyr Ala Thr Asn Ala Asn Gly Asn Ala Arg 515 520 525 Ile Lys Glu Phe Lys Glu Met Val Leu Ser Leu His Arg Glu His Ile 530 535 540 Gly Val Asn Met Asp Val Val Tyr Asn His Thr Phe Ala Thr Gln Ile 545 550 555 560 Ser Asp Phe Asp Lys Ile Val Pro Glu Tyr Tyr Tyr Arg Thr Asp Asp 565 570 575 Ala Gly Asn Tyr Thr Asn Gly Ser Gly Thr Gly Asn Glu Ile Ala Ala 580 585 590 Glu Arg Pro Met Val Gln Lys Phe Ile Ile Asp Ser Leu Lys Tyr Trp 595 600 605 Val Asn Glu Tyr His Ile Asp Gly Phe Arg Phe Asp Leu Met Ala Leu 610 615 620 Leu Gly Lys Asp Thr Met Ser Lys Ala Ala Ser Glu Leu His Ala Ile 625 630 635 640 Asn Pro Gly Ile Ala Leu Tyr Gly Glu Pro Trp Thr Gly Gly Thr Ser 645 650 655 Ala Leu Pro Asp Asp Gln Leu Leu Thr Lys Gly Ala Gln Lys Gly Met 660 665 670 Gly Val Ala Val Phe Asn Asp Asn Leu Arg Asn Ala Leu Asp Gly Asn 675 680 685 Val Phe Asp Ser Ser Ala Gln Gly Phe Ala Thr Gly Ala Thr Gly Leu 690 695 700 Thr Asp Ala Ile Lys Asn Gly Val Glu Gly Ser Ile Asn Asp Phe Thr 705 710 715 720 Ser Ser Pro Gly Glu Thr Ile Asn Tyr Val Thr Ser His Asp Asn Tyr 725 730 735 Thr Leu Trp Asp Lys Ile Ala Leu Ser Asn Pro Asn Asp Ser Glu Ala 740 745 750 Asp Arg Ile Lys Met Asp Glu Leu Ala Gln Ala Val Val Met Thr Ser 755 760 765 Gln Gly Val Pro Phe Met Gln Gly Gly Glu Glu Met Leu Arg Thr Lys 770 775 780 Gly Gly Asn Asp Asn Ser Tyr Asn Ala Gly Asp Ala Val Asn Glu Phe 785 790 795 800 Asp Trp Ser Arg Lys Ala Gln Tyr Pro Asp Val Phe Asn Tyr Tyr Ser 805 810 815 Gly Leu Ile His Leu Arg Leu Asp His Pro Ala Phe Arg Met Thr Thr 820 825 830 Ala Asn Glu Ile Asn Ser His Leu Gln Phe Leu Asn Ser Pro Glu Asn 835 840 845 Thr Val Ala Tyr Glu Leu Thr Asp His Val Asn Lys Asp Lys Trp Gly 850 855 860 Asn Ile Ile Val Val Tyr Asn Pro Asn Lys Thr Val Ala Thr Ile Asn 865 870 875 880 Leu Pro Ser Gly Lys Trp Ala Ile Asn Ala Thr Ser Gly Lys Val Gly 885 890 895 Glu Ser Thr Leu Gly Gln Ala Glu Gly Ser Val Gln Val Pro Gly Ile 900 905 910 Ser Met Met Ile Leu His Gln Glu Val Ser Pro Asp His Gly Lys Lys 915 920 925 5 2487 DNA Bacillius acidopullulyticus CDS (1)...(2487) 5 gat tct acc tcg aca gaa gtc att gtg cat tat cat cgt ttt gat tct 48 Asp Ser Thr Ser Thr Glu Val Ile Val His Tyr His Arg Phe Asp Ser 1 5 10 15 aac tat gca aat tgg gat cta tgg atg tgg cca tat caa cca gtt aat 96 Asn Tyr Ala Asn Trp Asp Leu Trp Met Trp Pro Tyr Gln Pro Val Asn 20 25 30 ggt aat gga gca gca tac gag ttt tct gga aag gat gat ttt ggc gtt 144 Gly Asn Gly Ala Ala Tyr Glu Phe Ser Gly Lys Asp Asp Phe Gly Val 35 40 45 aaa gca gat gtt caa gtg cct ggg gat gat aca cag gta ggt ctg att 192 Lys Ala Asp Val Gln Val Pro Gly Asp Asp Thr Gln Val Gly Leu Ile 50 55 60 gtc cgt aca aat gat tgg agc caa aaa aat aca tca gac gat ctc cat 240 Val Arg Thr Asn Asp Trp Ser Gln Lys Asn Thr Ser Asp Asp Leu His 65 70 75 80 att gat ctg aca aag ggg cat gaa ata tgg att gtt cag ggg gat ccc 288 Ile Asp Leu Thr Lys Gly His Glu Ile Trp Ile Val Gln Gly Asp Pro 85 90 95 aat att tat tac aat ctg agt gat gcg cag gct gca gcg act cca aag 336 Asn Ile Tyr Tyr Asn Leu Ser Asp Ala Gln Ala Ala Ala Thr Pro Lys 100 105 110 gtt tcg aat gcg tat ttg gat aat gaa aaa aca gta ttg gca aag cta 384 Val Ser Asn Ala Tyr Leu Asp Asn Glu Lys Thr Val Leu Ala Lys Leu 115 120 125 act aat cca atg aca tta tca gat gga tca agc ggc ttt acg gtt aca 432 Thr Asn Pro Met Thr Leu Ser Asp Gly Ser Ser Gly Phe Thr Val Thr 130 135 140 gat aaa aca aca ggg gaa caa att cca gtt acc gct gca aca aat gcg 480 Asp Lys Thr Thr Gly Glu Gln Ile Pro Val Thr Ala Ala Thr Asn Ala 145 150 155 160 aac tca gcc tcc tcg tct gag cag aca gac ttg gtt caa ttg acg tta 528 Asn Ser Ala Ser Ser Ser Glu Gln Thr Asp Leu Val Gln Leu Thr Leu 165 170 175 gcc agt gca ccg gat gtt tcc cat aca ata caa gta gga gca gcc ggt 576 Ala Ser Ala Pro Asp Val Ser His Thr Ile Gln Val Gly Ala Ala Gly 180 185 190 tat gaa gca gtc aat ctc ata cca cga aat gta tta aat ttg cct cgt 624 Tyr Glu Ala Val Asn Leu Ile Pro Arg Asn Val Leu Asn Leu Pro Arg 195 200 205 tat tat tac agc gga aat gat tta ggt aac gtt tat tca aat aag gca 672 Tyr Tyr Tyr Ser Gly Asn Asp Leu Gly Asn Val Tyr Ser Asn Lys Ala 210 215 220 acg gcc ttc cgt gta tgg gct cca act gct tcg gat gtc caa tta ctt 720 Thr Ala Phe Arg Val Trp Ala Pro Thr Ala Ser Asp Val Gln Leu Leu 225 230 235 240 tta tac aat agt gaa aca gga cct gta acc aaa cag ctt gaa atg caa 768 Leu Tyr Asn Ser Glu Thr Gly Pro Val Thr Lys Gln Leu Glu Met Gln 245 250 255 aag agt gat aac ggt aca tgg aaa ctg aag gtc cct ggt aat ctg aaa 816 Lys Ser Asp Asn Gly Thr Trp Lys Leu Lys Val Pro Gly Asn Leu Lys 260 265 270 aat tgg tat tat ctc tat cag gta acg gtg aat ggg aag aca caa aca 864 Asn Trp Tyr Tyr Leu Tyr Gln Val Thr Val Asn Gly Lys Thr Gln Thr 275 280 285 gcc gtt gac cct tat gtg cgt gct att tca gtc aat gca aca cgt ggt 912 Ala Val Asp Pro Tyr Val Arg Ala Ile Ser Val Asn Ala Thr Arg Gly 290 295 300 atg ata gtc gat tta gaa gat acg aat cct cct gga tgg aaa gaa gat 960 Met Ile Val Asp Leu Glu Asp Thr Asn Pro Pro Gly Trp Lys Glu Asp 305 310 315 320 cat caa cag aca cct gcg aac cca gtg gat gaa gta atc tac gaa gtg 1008 His Gln Gln Thr Pro Ala Asn Pro Val Asp Glu Val Ile Tyr Glu Val 325 330 335 cat gtg cgt gat ttt tcg att gat gct aat tca ggc atg aaa aat aaa 1056 His Val Arg Asp Phe Ser Ile Asp Ala Asn Ser Gly Met Lys Asn Lys 340 345 350 ggg aaa tat ctt gcc ttt aca gaa cat ggc aca aaa ggc cct gat aac 1104 Gly Lys Tyr Leu Ala Phe Thr Glu His Gly Thr Lys Gly Pro Asp Asn 355 360 365 gtg aaa acg ggt att gat agt ttg aag gaa tta gga atc aat gct gtt 1152 Val Lys Thr Gly Ile Asp Ser Leu Lys Glu Leu Gly Ile Asn Ala Val 370 375 380 caa tta cag ccg att gaa gaa ttt aac agc att gat gaa acc caa cca 1200 Gln Leu Gln Pro Ile Glu Glu Phe Asn Ser Ile Asp Glu Thr Gln Pro 385 390 395 400 aat atg tat aac tgg ggc tat gac cca aga aac tac aac gtc cct gaa 1248 Asn Met Tyr Asn Trp Gly Tyr Asp Pro Arg Asn Tyr Asn Val Pro Glu 405 410 415 gga gcg tat gca act aca cca gaa gga acg gct cgc att acc cag tta 1296 Gly Ala Tyr Ala Thr Thr Pro Glu Gly Thr Ala Arg Ile Thr Gln Leu 420 425 430 aag caa ctg att caa agc att cat aaa gat cgg att gct atc aat atg 1344 Lys Gln Leu Ile Gln Ser Ile His Lys Asp Arg Ile Ala Ile Asn Met 435 440 445 gat gtg gtc tat aac cat acc ttt aac gta gga gtg tct gat ttt gat 1392 Asp Val Val Tyr Asn His Thr Phe Asn Val Gly Val Ser Asp Phe Asp 450 455 460 aag att gtt ccg caa tac tat tat cgg aca gac agc gca ggt aat tat 1440 Lys Ile Val Pro Gln Tyr Tyr Tyr Arg Thr Asp Ser Ala Gly Asn Tyr 465 470 475 480 acg aac ggc tca ggt gta ggt aat gaa att gcg acc gag cgt ccg atg 1488 Thr Asn Gly Ser Gly Val Gly Asn Glu Ile Ala Thr Glu Arg Pro Met 485 490 495 gtc caa aag ttc gtt ctg gat tct gtt aaa tat tgg gta aag gaa tac 1536 Val Gln Lys Phe Val Leu Asp Ser Val Lys Tyr Trp Val Lys Glu Tyr 500 505 510 cat atc gac ggc ttc cgt ttc gat ctt atg gct ctt tta gga aaa gac 1584 His Ile Asp Gly Phe Arg Phe Asp Leu Met Ala Leu Leu Gly Lys Asp 515 520 525 acc atg gcc aaa ata tca aaa gag ctt cat gct att aat cct ggc att 1632 Thr Met Ala Lys Ile Ser Lys Glu Leu His Ala Ile Asn Pro Gly Ile 530 535 540 gtc ctg tat gga gaa cca tgg act ggc ggt acc tct gga tta tca agc 1680 Val Leu Tyr Gly Glu Pro Trp Thr Gly Gly Thr Ser Gly Leu Ser Ser 545 550 555 560 gac caa ctc gtt acg aaa ggt cag caa aag ggc ttg gga att ggc gta 1728 Asp Gln Leu Val Thr Lys Gly Gln Gln Lys Gly Leu Gly Ile Gly Val 565 570 575 ttc aac gat aat att cgg aac gga ctc gat ggt aac gtt ttt gat aaa 1776 Phe Asn Asp Asn Ile Arg Asn Gly Leu Asp Gly Asn Val Phe Asp Lys 580 585 590 tcg gca caa gga ttt gca aca gga gat cca aac caa gtt aat gtc att 1824 Ser Ala Gln Gly Phe Ala Thr Gly Asp Pro Asn Gln Val Asn Val Ile 595 600 605 aaa aat aga gtt atg gga agt att tca gat ttc act tcg gca cct agc 1872 Lys Asn Arg Val Met Gly Ser Ile Ser Asp Phe Thr Ser Ala Pro Ser 610 615 620 gaa acc att aac tat gta aca agc cat gat aat atg aca ttg tgg gat 1920 Glu Thr Ile Asn Tyr Val Thr Ser His Asp Asn Met Thr Leu Trp Asp 625 630 635 640 aaa att agc gca agt aat ccg aac gat aca caa gca gat cga att aag 1968 Lys Ile Ser Ala Ser Asn Pro Asn Asp Thr Gln Ala Asp Arg Ile Lys 645 650 655 atg gat gaa ttg gct caa gct gtg gta ttt act tca caa ggg gta cca 2016 Met Asp Glu Leu Ala Gln Ala Val Val Phe Thr Ser Gln Gly Val Pro 660 665 670 ttt atg caa ggt gga gaa gaa atg ctg cgg aca aaa ggc ggt aat gat 2064 Phe Met Gln Gly Gly Glu Glu Met Leu Arg Thr Lys Gly Gly Asn Asp 675 680 685 aat agt tac aat gcc ggg gat agc gtg aat cag ttc gat tgg tca aga 2112 Asn Ser Tyr Asn Ala Gly Asp Ser Val Asn Gln Phe Asp Trp Ser Arg 690 695 700 aaa gca caa ttt gaa aat gta ttc gac tac tat tct tgg ttg att cat 2160 Lys Ala Gln Phe Glu Asn Val Phe Asp Tyr Tyr Ser Trp Leu Ile His 705 710 715 720 cta cgt gat aat cac cca gca ttc cgt atg acg aca gcg gat caa atc 2208 Leu Arg Asp Asn His Pro Ala Phe Arg Met Thr Thr Ala Asp Gln Ile 725 730 735 aaa caa aat ctc act ttc ttg gat agc cca acg aac act gta gca ttt 2256 Lys Gln Asn Leu Thr Phe Leu Asp Ser Pro Thr Asn Thr Val Ala Phe 740 745 750 gaa tta aaa aat cat gcc aat cat gat aaa tgg aaa aac att ata gtt 2304 Glu Leu Lys Asn His Ala Asn His Asp Lys Trp Lys Asn Ile Ile Val 755 760 765 atg tat aat cca aat aaa act gca caa act ctc act cta cca agt gga 2352 Met Tyr Asn Pro Asn Lys Thr Ala Gln Thr Leu Thr Leu Pro Ser Gly 770 775 780 aat tgg aca att gta gga tta ggc aat caa gta ggt gag aaa tca cta 2400 Asn Trp Thr Ile Val Gly Leu Gly Asn Gln Val Gly Glu Lys Ser Leu 785 790 795 800 ggc cat gta aat ggc acg gtt gag gtg cca gct ctt agt acg atc att 2448 Gly His Val Asn Gly Thr Val Glu Val Pro Ala Leu Ser Thr Ile Ile 805 810 815 ctt cat cag ggt aca tct gaa gat gtc att gat caa aat 2487 Leu His Gln Gly Thr Ser Glu Asp Val Ile Asp Gln Asn 820 825 6 829 PRT Bacillius acidopullulyticus 6 Asp Ser Thr Ser Thr Glu Val Ile Val His Tyr His Arg Phe Asp Ser 1 5 10 15 Asn Tyr Ala Asn Trp Asp Leu Trp Met Trp Pro Tyr Gln Pro Val Asn 20 25 30 Gly Asn Gly Ala Ala Tyr Glu Phe Ser Gly Lys Asp Asp Phe Gly Val 35 40 45 Lys Ala Asp Val Gln Val Pro Gly Asp Asp Thr Gln Val Gly Leu Ile 50 55 60 Val Arg Thr Asn Asp Trp Ser Gln Lys Asn Thr Ser Asp Asp Leu His 65 70 75 80 Ile Asp Leu Thr Lys Gly His Glu Ile Trp Ile Val Gln Gly Asp Pro 85 90 95 Asn Ile Tyr Tyr Asn Leu Ser Asp Ala Gln Ala Ala Ala Thr Pro Lys 100 105 110 Val Ser Asn Ala Tyr Leu Asp Asn Glu Lys Thr Val Leu Ala Lys Leu 115 120 125 Thr Asn Pro Met Thr Leu Ser Asp Gly Ser Ser Gly Phe Thr Val Thr 130 135 140 Asp Lys Thr Thr Gly Glu Gln Ile Pro Val Thr Ala Ala Thr Asn Ala 145 150 155 160 Asn Ser Ala Ser Ser Ser Glu Gln Thr Asp Leu Val Gln Leu Thr Leu 165 170 175 Ala Ser Ala Pro Asp Val Ser His Thr Ile Gln Val Gly Ala Ala Gly 180 185 190 Tyr Glu Ala Val Asn Leu Ile Pro Arg Asn Val Leu Asn Leu Pro Arg 195 200 205 Tyr Tyr Tyr Ser Gly Asn Asp Leu Gly Asn Val Tyr Ser Asn Lys Ala 210 215 220 Thr Ala Phe Arg Val Trp Ala Pro Thr Ala Ser Asp Val Gln Leu Leu 225 230 235 240 Leu Tyr Asn Ser Glu Thr Gly Pro Val Thr Lys Gln Leu Glu Met Gln 245 250 255 Lys Ser Asp Asn Gly Thr Trp Lys Leu Lys Val Pro Gly Asn Leu Lys 260 265 270 Asn Trp Tyr Tyr Leu Tyr Gln Val Thr Val Asn Gly Lys Thr Gln Thr 275 280 285 Ala Val Asp Pro Tyr Val Arg Ala Ile Ser Val Asn Ala Thr Arg Gly 290 295 300 Met Ile Val Asp Leu Glu Asp Thr Asn Pro Pro Gly Trp Lys Glu Asp 305 310 315 320 His Gln Gln Thr Pro Ala Asn Pro Val Asp Glu Val Ile Tyr Glu Val 325 330 335 His Val Arg Asp Phe Ser Ile Asp Ala Asn Ser Gly Met Lys Asn Lys 340 345 350 Gly Lys Tyr Leu Ala Phe Thr Glu His Gly Thr Lys Gly Pro Asp Asn 355 360 365 Val Lys Thr Gly Ile Asp Ser Leu Lys Glu Leu Gly Ile Asn Ala Val 370 375 380 Gln Leu Gln Pro Ile Glu Glu Phe Asn Ser Ile Asp Glu Thr Gln Pro 385 390 395 400 Asn Met Tyr Asn Trp Gly Tyr Asp Pro Arg Asn Tyr Asn Val Pro Glu 405 410 415 Gly Ala Tyr Ala Thr Thr Pro Glu Gly Thr Ala Arg Ile Thr Gln Leu 420 425 430 Lys Gln Leu Ile Gln Ser Ile His Lys Asp Arg Ile Ala Ile Asn Met 435 440 445 Asp Val Val Tyr Asn His Thr Phe Asn Val Gly Val Ser Asp Phe Asp 450 455 460 Lys Ile Val Pro Gln Tyr Tyr Tyr Arg Thr Asp Ser Ala Gly Asn Tyr 465 470 475 480 Thr Asn Gly Ser Gly Val Gly Asn Glu Ile Ala Thr Glu Arg Pro Met 485 490 495 Val Gln Lys Phe Val Leu Asp Ser Val Lys Tyr Trp Val Lys Glu Tyr 500 505 510 His Ile Asp Gly Phe Arg Phe Asp Leu Met Ala Leu Leu Gly Lys Asp 515 520 525 Thr Met Ala Lys Ile Ser Lys Glu Leu His Ala Ile Asn Pro Gly Ile 530 535 540 Val Leu Tyr Gly Glu Pro Trp Thr Gly Gly Thr Ser Gly Leu Ser Ser 545 550 555 560 Asp Gln Leu Val Thr Lys Gly Gln Gln Lys Gly Leu Gly Ile Gly Val 565 570 575 Phe Asn Asp Asn Ile Arg Asn Gly Leu Asp Gly Asn Val Phe Asp Lys 580 585 590 Ser Ala Gln Gly Phe Ala Thr Gly Asp Pro Asn Gln Val Asn Val Ile 595 600 605 Lys Asn Arg Val Met Gly Ser Ile Ser Asp Phe Thr Ser Ala Pro Ser 610 615 620 Glu Thr Ile Asn Tyr Val Thr Ser His Asp Asn Met Thr Leu Trp Asp 625 630 635 640 Lys Ile Ser Ala Ser Asn Pro Asn Asp Thr Gln Ala Asp Arg Ile Lys 645 650 655 Met Asp Glu Leu Ala Gln Ala Val Val Phe Thr Ser Gln Gly Val Pro 660 665 670 Phe Met Gln Gly Gly Glu Glu Met Leu Arg Thr Lys Gly Gly Asn Asp 675 680 685 Asn Ser Tyr Asn Ala Gly Asp Ser Val Asn Gln Phe Asp Trp Ser Arg 690 695 700 Lys Ala Gln Phe Glu Asn Val Phe Asp Tyr Tyr Ser Trp Leu Ile His 705 710 715 720 Leu Arg Asp Asn His Pro Ala Phe Arg Met Thr Thr Ala Asp Gln Ile 725 730 735 Lys Gln Asn Leu Thr Phe Leu Asp Ser Pro Thr Asn Thr Val Ala Phe 740 745 750 Glu Leu Lys Asn His Ala Asn His Asp Lys Trp Lys Asn Ile Ile Val 755 760 765 Met Tyr Asn Pro Asn Lys Thr Ala Gln Thr Leu Thr Leu Pro Ser Gly 770 775 780 Asn Trp Thr Ile Val Gly Leu Gly Asn Gln Val Gly Glu Lys Ser Leu 785 790 795 800 Gly His Val Asn Gly Thr Val Glu Val Pro Ala Leu Ser Thr Ile Ile 805 810 815 Leu His Gln Gly Thr Ser Glu Asp Val Ile Asp Gln Asn 820 825 7 23 DNA Artificial Sequence Primer 7 cgcttcggaa tcattaggat tgc 23 8 27 DNA Artificial Sequence Primer 8 gcttccgttt tgccttaatg gcgctgc 27 9 23 DNA Artificial Sequence Primer 9 ggccaaggct ctacccgaac ggc 23 10 26 DNA Artificial Sequence Primer 10 gcactttacg gggcgccatg gacggg 26 

What is claimed is:
 1. An isolated pullulanase variant, wherein (a) the variant is at least 50% homologous to SEQ ID NO:2; (b) the variant comprises an amino acid modification compared to SEQ ID NO:1 in at least one of the positions corresponding to 95-113, K122P, 130-140, K151P, 157-165, 180, 181, 210, 227, 228, 232-238, 259, 266-272, 286, G293P, 298, 299, 300-314, N315P, 337-339, 353, N374P, 380, 384, 385, 392, 394, 396, 406, 408-429, 442, A446P, 478, 500-507, 515, 526, 534, 543, 544 550, T556P, 557, 563, 568, 573, 576, 583, 627, 659-665, G668P, G672P, 681, 684, 688, 689, 751-755, 732, 736, 740, 760, 767, 770 783, 788, 792, 793, K758C+I914C, T916C+A765C, I897C+S819C, P525C+E499C and H286C+T148C; and (c) the variant has an improved thermostability as compared to the parent pullulanase.
 2. The variant according to claim 1, wherein the improved thermostability is defined by an increased half-life (T_(½)) of at least about 5% in a “T_(½) assay for liquefaction”, using a pH of 5.0 and a temperature of 95° C.
 3. The variant according to claim 1, wherein the improved thermostability is defined by an increased residual enzyme activity of at least about 5% in an “assay for residual activity after liquefaction” using a pH of 5.0 and a temperature of 95° C.
 4. The variant according to claim 1, wherein the improved thermostability is defined by an increased half-life (T_(½)) of at least about 5% in a “T_(½) assay for saccharification”, using a pH of 4.5 and a temperature of 70° C.
 5. The variant according to claim 1, wherein the improved thermostability is defined by an increased residual enzyme activity of at least about 5% in an “assay for residual activity after saccharification”, using a pH of 4.5 and a temperature of 63° C.
 6. The variant according to claim 5, wherein the “assay for activity for saccharification” is carried out at a pH of 4.5 and at a temperature of 70° C.
 7. The variant according to claim 1, wherein the variant further has an increased isoamylase activity as compared to the parent pullulanase.
 8. The variant according to claim 1, wherein the variant further has an altered pH dependent activity as compared to the parent pullulanase. 